PubMed:15342552
Annnotations
Glycan-Motif
{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":87,"end":96},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":87,"end":96},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":271,"end":280},"obj":"https://glytoucan.org/Structures/Glycans/G00061MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos6-Glycan-Motif-Image
{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":87,"end":96},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":271,"end":280},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00061MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"TextSentencer_T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"TextSentencer_T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"TextSentencer_T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"TextSentencer_T18","span":{"begin":2607,"end":2715},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"T18","span":{"begin":2607,"end":2715},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"T18","span":{"begin":2607,"end":2715},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos6-Glycan-Motif-Structure
{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":87,"end":96},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":87,"end":96},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":271,"end":280},"obj":"https://glytoucan.org/Structures/Glycans/G00061MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
Glycosmos6-GlycoEpitope
{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":271,"end":280},"obj":"http://www.glycoepitope.jp/epitopes/EP0073"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
Glycosmos6-MAT
{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
uniprot-human
{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":151,"end":153},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T2","span":{"begin":777,"end":779},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T3","span":{"begin":944,"end":946},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T4","span":{"begin":1228,"end":1230},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T5","span":{"begin":1756,"end":1758},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T6","span":{"begin":1829,"end":1831},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T7","span":{"begin":1863,"end":1865},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T8","span":{"begin":1905,"end":1907},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T9","span":{"begin":1969,"end":1971},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T10","span":{"begin":2003,"end":2005},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T11","span":{"begin":2069,"end":2071},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T12","span":{"begin":2124,"end":2126},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T13","span":{"begin":2191,"end":2193},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T14","span":{"begin":2210,"end":2212},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T15","span":{"begin":2332,"end":2334},"obj":"http://www.uniprot.org/uniprot/P40967"},{"id":"T16","span":{"begin":151,"end":153},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T17","span":{"begin":777,"end":779},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T18","span":{"begin":944,"end":946},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T19","span":{"begin":1228,"end":1230},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T20","span":{"begin":1756,"end":1758},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T21","span":{"begin":1829,"end":1831},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T22","span":{"begin":1863,"end":1865},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T23","span":{"begin":1905,"end":1907},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T24","span":{"begin":1969,"end":1971},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T25","span":{"begin":2003,"end":2005},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T26","span":{"begin":2069,"end":2071},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T27","span":{"begin":2124,"end":2126},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T28","span":{"begin":2191,"end":2193},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T29","span":{"begin":2210,"end":2212},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T30","span":{"begin":2332,"end":2334},"obj":"http://www.uniprot.org/uniprot/P14222"},{"id":"T31","span":{"begin":151,"end":153},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T32","span":{"begin":777,"end":779},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T33","span":{"begin":944,"end":946},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T34","span":{"begin":1228,"end":1230},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T35","span":{"begin":1756,"end":1758},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T36","span":{"begin":1829,"end":1831},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T37","span":{"begin":1863,"end":1865},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T38","span":{"begin":1905,"end":1907},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T39","span":{"begin":1969,"end":1971},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T40","span":{"begin":2003,"end":2005},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T41","span":{"begin":2069,"end":2071},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T42","span":{"begin":2124,"end":2126},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T43","span":{"begin":2191,"end":2193},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T44","span":{"begin":2210,"end":2212},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T45","span":{"begin":2332,"end":2334},"obj":"http://www.uniprot.org/uniprot/Q9H1E3"},{"id":"T46","span":{"begin":1318,"end":1331},"obj":"http://www.uniprot.org/uniprot/Q86YG0"},{"id":"T47","span":{"begin":1859,"end":1861},"obj":"http://www.uniprot.org/uniprot/P04554"},{"id":"T48","span":{"begin":2029,"end":2031},"obj":"http://www.uniprot.org/uniprot/P04554"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
uniprot-mouse
{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":151,"end":153},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T2","span":{"begin":777,"end":779},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T3","span":{"begin":944,"end":946},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T4","span":{"begin":1228,"end":1230},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T5","span":{"begin":1756,"end":1758},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T6","span":{"begin":1829,"end":1831},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T7","span":{"begin":1863,"end":1865},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T8","span":{"begin":1905,"end":1907},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T9","span":{"begin":1969,"end":1971},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T10","span":{"begin":2003,"end":2005},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T11","span":{"begin":2069,"end":2071},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T12","span":{"begin":2124,"end":2126},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T13","span":{"begin":2191,"end":2193},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T14","span":{"begin":2210,"end":2212},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T15","span":{"begin":2332,"end":2334},"obj":"http://www.uniprot.org/uniprot/P10820"},{"id":"T16","span":{"begin":1318,"end":1331},"obj":"http://www.uniprot.org/uniprot/P07724"},{"id":"T17","span":{"begin":1333,"end":1336},"obj":"http://www.uniprot.org/uniprot/P24807"},{"id":"T18","span":{"begin":1859,"end":1861},"obj":"http://www.uniprot.org/uniprot/Q9R0C0"},{"id":"T19","span":{"begin":2029,"end":2031},"obj":"http://www.uniprot.org/uniprot/Q9R0C0"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlycoBiology-NCBITAXON
{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":122,"end":132},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T2","span":{"begin":1235,"end":1245},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T3","span":{"begin":1624,"end":1629},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T4","span":{"begin":2053,"end":2063},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T5","span":{"begin":2175,"end":2185},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":203,"end":215},"obj":"http://purl.obolibrary.org/obo/GO_0000752"},{"id":"T2","span":{"begin":203,"end":215},"obj":"http://purl.obolibrary.org/obo/GO_0007157"},{"id":"T3","span":{"begin":230,"end":234},"obj":"http://purl.obolibrary.org/obo/GO_0004617"},{"id":"T4","span":{"begin":461,"end":465},"obj":"http://purl.obolibrary.org/obo/GO_0004617"},{"id":"T5","span":{"begin":1846,"end":1850},"obj":"http://purl.obolibrary.org/obo/GO_0004617"},{"id":"T6","span":{"begin":589,"end":598},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T7","span":{"begin":1338,"end":1347},"obj":"http://purl.obolibrary.org/obo/GO_0000746"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":22,"end":32},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T2","span":{"begin":154,"end":164},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T3","span":{"begin":396,"end":406},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T4","span":{"begin":417,"end":427},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T5","span":{"begin":831,"end":841},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T6","span":{"begin":861,"end":871},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T7","span":{"begin":1060,"end":1070},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T8","span":{"begin":1255,"end":1265},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T9","span":{"begin":1404,"end":1414},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T10","span":{"begin":1519,"end":1529},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T11","span":{"begin":1908,"end":1918},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T12","span":{"begin":1972,"end":1982},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T13","span":{"begin":2335,"end":2345},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T14","span":{"begin":2416,"end":2426},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T15","span":{"begin":2521,"end":2531},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T16","span":{"begin":540,"end":548},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T17","span":{"begin":549,"end":556},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T18","span":{"begin":549,"end":556},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":549,"end":556},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T20","span":{"begin":549,"end":556},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":138,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T2","span":{"begin":175,"end":178},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T3","span":{"begin":413,"end":416},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T4","span":{"begin":560,"end":563},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T5","span":{"begin":671,"end":674},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T6","span":{"begin":700,"end":703},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T7","span":{"begin":827,"end":830},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T8","span":{"begin":920,"end":923},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T9","span":{"begin":954,"end":957},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T10","span":{"begin":1152,"end":1155},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T11","span":{"begin":1164,"end":1167},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T12","span":{"begin":1251,"end":1254},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T13","span":{"begin":1304,"end":1307},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T14","span":{"begin":1400,"end":1403},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T15","span":{"begin":1441,"end":1444},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T16","span":{"begin":1515,"end":1518},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T17","span":{"begin":1610,"end":1613},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T18","span":{"begin":2155,"end":2158},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T19","span":{"begin":2167,"end":2170},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T20","span":{"begin":2236,"end":2239},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T21","span":{"begin":2319,"end":2322},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T22","span":{"begin":2457,"end":2460},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T23","span":{"begin":2517,"end":2520},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T24","span":{"begin":2602,"end":2605},"obj":"http://purl.obolibrary.org/obo/GO_0005731"},{"id":"T25","span":{"begin":584,"end":587},"obj":"http://purl.obolibrary.org/obo/GO_1990295"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
UBERON-AE
{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1318,"end":1323},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"T2","span":{"begin":2020,"end":2025},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"T3","span":{"begin":2353,"end":2358},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"T4","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlycoBiology-MAT
{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T2","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T3","span":{"begin":1656,"end":1662},"obj":"http://purl.obolibrary.org/obo/MAT_0000488"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlycoBiology-Motifs
{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":1618,"end":1629},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
performance-test
{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1618,"end":1623},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1318,"end":1323},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":2020,"end":2025},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":2353,"end":2358},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlycoBiology-Epitope
{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":271,"end":280},"obj":"http://www.glycoepitope.jp/epitopes/EP0073"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyTouCan-IUPAC
{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T2","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T3","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T4","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T5","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T6","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T7","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G44384WF\""},{"id":"GlycanIUPAC_T8","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T9","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T10","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T11","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T12","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T13","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T14","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G37452RG\""},{"id":"GlycanIUPAC_T15","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T16","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T17","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T18","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T19","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T20","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T21","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G56296FC\""},{"id":"GlycanIUPAC_T22","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T23","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T24","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T25","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T26","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T27","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T28","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G44877OG\""},{"id":"GlycanIUPAC_T29","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T30","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T31","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T32","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T33","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T34","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T35","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G22627HB\""},{"id":"GlycanIUPAC_T36","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T37","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T38","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T39","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T40","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T41","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T42","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G76069IP\""},{"id":"GlycanIUPAC_T43","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T44","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T45","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T46","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T47","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T48","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T49","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G77301LL\""},{"id":"GlycanIUPAC_T50","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T51","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T52","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T53","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T54","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T55","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T56","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G92446EV\""},{"id":"GlycanIUPAC_T57","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T58","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T59","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T60","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T61","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T62","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T63","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G93798MG\""},{"id":"GlycanIUPAC_T64","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T65","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T66","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T67","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T68","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T69","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T70","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G19180VS\""},{"id":"GlycanIUPAC_T71","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T72","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T73","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T74","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T75","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T76","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T77","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G00261CT\""},{"id":"GlycanIUPAC_T78","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T79","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T80","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T81","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T82","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T83","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T84","span":{"begin":2159,"end":2162},"obj":"\"http://rdf.glycoinfo.org/glycan/G23925MM\""},{"id":"GlycanIUPAC_T85","span":{"begin":564,"end":567},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T86","span":{"begin":675,"end":678},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T87","span":{"begin":924,"end":927},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T88","span":{"begin":1156,"end":1159},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T89","span":{"begin":1308,"end":1311},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T90","span":{"begin":2127,"end":2130},"obj":"\"http://rdf.glycoinfo.org/glycan/G27176LA\""},{"id":"GlycanIUPAC_T91","span":{"begin":2159,"end":21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lycanIUPAC_T1304","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T1305","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T1306","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T1307","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T1308","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T1309","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T1310","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T1311","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T1312","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T1313","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T1314","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T1315","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T1316","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T1317","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T1318","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T1319","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T1320","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T1321","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T1322","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T1323","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T1324","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T1325","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T1326","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T1327","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T1328","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T1329","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T1330","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T1331","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T1332","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T1333","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T1334","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T1335","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T1336","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T1337","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T1338","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T1339","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T1340","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T1341","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T1342","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T1343","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T1344","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T1345","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T1346","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T1347","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T1348","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T1349","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T1350","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T1351","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T1352","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T1353","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T1354","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T1355","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T1356","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T1357","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T1358","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T1359","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T1360","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T1361","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T1362","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T1363","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T1364","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T1365","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T1366","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T1367","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T1368","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T1369","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T1370","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T1371","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T1372","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T1373","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T1374","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T1375","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T1376","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T1377","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T1378","span":{"begin":1391,"end":1394},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""},{"id":"GlycanIUPAC_T1379","span":{"begin":1728,"end":1731},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
mondo_disease
{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":1333,"end":1336},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0011848"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
Anatomy-MAT
{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1618,"end":1623},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
Glycan-GlyCosmos
{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":271,"end":280},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00061MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00061MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos-GlycoEpitope
{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":271,"end":280},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0073"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-CL
{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":179,"end":191},"obj":"Cell"},{"id":"T2","span":{"begin":1739,"end":1751},"obj":"Cell"},{"id":"T3","span":{"begin":1832,"end":1844},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000232"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-UBERON
{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":179,"end":191},"obj":"Body_part"},{"id":"T2","span":{"begin":1465,"end":1470},"obj":"Body_part"},{"id":"T4","span":{"begin":1618,"end":1623},"obj":"Body_part"},{"id":"T5","span":{"begin":1739,"end":1751},"obj":"Body_part"},{"id":"T6","span":{"begin":1832,"end":1844},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000119"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0022303"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000232"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-MAT
{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":1618,"end":1623},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"TextSentencer_T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"TextSentencer_T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"TextSentencer_T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"TextSentencer_T18","span":{"begin":2607,"end":2715},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"T18","span":{"begin":2607,"end":2715},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"T18","span":{"begin":2607,"end":2715},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-Sentences
{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T2","span":{"begin":166,"end":407},"obj":"Sentence"},{"id":"T3","span":{"begin":408,"end":784},"obj":"Sentence"},{"id":"T4","span":{"begin":785,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1052},"obj":"Sentence"},{"id":"T6","span":{"begin":1053,"end":1234},"obj":"Sentence"},{"id":"T7","span":{"begin":1235,"end":1390},"obj":"Sentence"},{"id":"T8","span":{"begin":1391,"end":1478},"obj":"Sentence"},{"id":"T9","span":{"begin":1479,"end":1651},"obj":"Sentence"},{"id":"T10","span":{"begin":1652,"end":1845},"obj":"Sentence"},{"id":"T11","span":{"begin":1846,"end":1919},"obj":"Sentence"},{"id":"T12","span":{"begin":1920,"end":1983},"obj":"Sentence"},{"id":"T13","span":{"begin":1984,"end":2174},"obj":"Sentence"},{"id":"T14","span":{"begin":2175,"end":2252},"obj":"Sentence"},{"id":"T15","span":{"begin":2253,"end":2346},"obj":"Sentence"},{"id":"T16","span":{"begin":2347,"end":2461},"obj":"Sentence"},{"id":"T17","span":{"begin":2462,"end":2606},"obj":"Sentence"},{"id":"T18","span":{"begin":2607,"end":2715},"obj":"Sentence"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-Glycan
{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":271,"end":280},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00061MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00061MO"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-GlycoEpitope
{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":271,"end":280},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0073"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
GlyCosmos15-NCBITAXON
{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":98,"end":103},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":116,"end":121},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":224,"end":229},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":390,"end":395},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":455,"end":460},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1294,"end":1298},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1312,"end":1317},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1992,"end":1997},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":2047,"end":2052},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":2347,"end":2352},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10090"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9606"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10088"},{"id":"A8","pred":"db_id","subj":"T8","obj":"9606"},{"id":"A9","pred":"db_id","subj":"T9","obj":"9606"},{"id":"A10","pred":"db_id","subj":"T10","obj":"10088"},{"id":"A11","pred":"db_id","subj":"T10","obj":"10090"},{"id":"A12","pred":"db_id","subj":"T12","obj":"9606"}],"namespaces":[{"prefix":"_base","uri":"http://purl.obolibrary.org/obo/NCBITaxon_"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
NCBITAXON
{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":98,"end":103},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":116,"end":121},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":224,"end":229},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":390,"end":395},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":455,"end":460},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1294,"end":1298},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1312,"end":1317},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1992,"end":1997},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":2047,"end":2052},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":2347,"end":2352},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10090"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9606"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10088"},{"id":"A8","pred":"db_id","subj":"T8","obj":"9606"},{"id":"A9","pred":"db_id","subj":"T9","obj":"9606"},{"id":"A10","pred":"db_id","subj":"T10","obj":"10088"},{"id":"A11","pred":"db_id","subj":"T10","obj":"10090"},{"id":"A12","pred":"db_id","subj":"T12","obj":"9606"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":179,"end":191},"obj":"Body_part"},{"id":"T2","span":{"begin":1465,"end":1470},"obj":"Body_part"},{"id":"T4","span":{"begin":1618,"end":1623},"obj":"Body_part"},{"id":"T5","span":{"begin":1739,"end":1751},"obj":"Body_part"},{"id":"T6","span":{"begin":1832,"end":1844},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000119"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0022303"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000232"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}
CL-cell
{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":179,"end":191},"obj":"Cell"},{"id":"T2","span":{"begin":1739,"end":1751},"obj":"Cell"},{"id":"T3","span":{"begin":1832,"end":1844},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000232"}],"text":"Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.\nThe rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Galalpha1-4GalNAcbeta1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures, and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), Galalpha1-4GalNAc (NOR-di), Galalpha1-4Galbeta1-3Galbeta1-4Glc ((Gal)3Glc), and Galalpha1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Galalpha1-4Gal/GalNAcbeta1-3Gal. Type 2 antibodies were specific to Galalpha1-4GalNAc, because they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-human serum albumin (HSA) conjugate and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Galalpha1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Galalpha1-4Galbeta1-4Glc-Cer) present in all normal erythrocytes and P1 (Galalpha1-4Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Galalpha1-4Galbeta1-4GlcNAc (P1-tri) and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to Pk and P1 glycolipids and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti-alpha-galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti-alpha-galactosyl antibodies still awaits elucidation."}