PubMed:3731182 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":241},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":242,"end":635},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":636,"end":954},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":955,"end":1232},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1233,"end":1511},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1512,"end":1625},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":241},"obj":"Sentence"},{"id":"T2","span":{"begin":242,"end":635},"obj":"Sentence"},{"id":"T3","span":{"begin":636,"end":954},"obj":"Sentence"},{"id":"T4","span":{"begin":955,"end":1232},"obj":"Sentence"},{"id":"T5","span":{"begin":1233,"end":1511},"obj":"Sentence"},{"id":"T6","span":{"begin":1512,"end":1625},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The effect of a \"bisecting\" N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-120) immobilized on agarose.\nThe effect of a \"bisecting\" 2-acetamido-2-deoxy-beta-D-glucopyranosyl group, linked (1----4) to the beta-D-mannopyranosyl group of asparagine-linked complex and hybrid oligosaccharides, on the binding of [14C]acetylated glycopeptides to columns of immobilized concanavalin A (Con A), Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin-120 (RCA-120) was investigated. The presence of this \"bisecting\" GlcNAc group caused significant inhibition of the binding to ConA-agarose of biantennary complex glycopeptides in which the two branches are terminated at their nonreducing ends by two GlcNAc groups, or by a Gal and a GlcNAc group, or by two Gal groups, or by a Man and a GlcNAc group. Binding of biantennary, complex glycopeptides to E-PHA-agarose required a \"bisecting\" GlcNAc group, a Gal group at the nonreducing terminus of the alpha-D-Man-p-(1----6) branch, and a terminal or internal GlcNAc residue linked beta-(1----2) to the alpha-D-Manp-(1----3) branch. Binding to RCA-120-agarose occurred only when at least one nonreducing terminal Gal group was present, and increased as the proportion of terminal Gal groups increased; the presence of a \"bisecting\" GlcNAc group caused either enhancement or inhibition of these binding patterns. It is concluded that a \"bisecting\" GlcNAc group affects the binding of glycopeptides to all three lectin columns."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":28,"end":48},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":669,"end":675},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":854,"end":860},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":887,"end":893},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":941,"end":947},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T6","span":{"begin":1041,"end":1047},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T7","span":{"begin":1160,"end":1166},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T8","span":{"begin":1432,"end":1438},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T9","span":{"begin":1547,"end":1553},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"The effect of a \"bisecting\" N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-120) immobilized on agarose.\nThe effect of a \"bisecting\" 2-acetamido-2-deoxy-beta-D-glucopyranosyl group, linked (1----4) to the beta-D-mannopyranosyl group of asparagine-linked complex and hybrid oligosaccharides, on the binding of [14C]acetylated glycopeptides to columns of immobilized concanavalin A (Con A), Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin-120 (RCA-120) was investigated. The presence of this \"bisecting\" GlcNAc group caused significant inhibition of the binding to ConA-agarose of biantennary complex glycopeptides in which the two branches are terminated at their nonreducing ends by two GlcNAc groups, or by a Gal and a GlcNAc group, or by two Gal groups, or by a Man and a GlcNAc group. Binding of biantennary, complex glycopeptides to E-PHA-agarose required a \"bisecting\" GlcNAc group, a Gal group at the nonreducing terminus of the alpha-D-Man-p-(1----6) branch, and a terminal or internal GlcNAc residue linked beta-(1----2) to the alpha-D-Manp-(1----3) branch. Binding to RCA-120-agarose occurred only when at least one nonreducing terminal Gal group was present, and increased as the proportion of terminal Gal groups increased; the presence of a \"bisecting\" GlcNAc group caused either enhancement or inhibition of these binding patterns. It is concluded that a \"bisecting\" GlcNAc group affects the binding of glycopeptides to all three lectin columns."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":170,"end":173},"obj":"Disease"},{"id":"T3","span":{"begin":566,"end":569},"obj":"Disease"},{"id":"T5","span":{"begin":1006,"end":1009},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0007710"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0008214"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0007710"},{"id":"A4","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0008214"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0007710"},{"id":"A6","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0008214"}],"text":"The effect of a \"bisecting\" N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-120) immobilized on agarose.\nThe effect of a \"bisecting\" 2-acetamido-2-deoxy-beta-D-glucopyranosyl group, linked (1----4) to the beta-D-mannopyranosyl group of asparagine-linked complex and hybrid oligosaccharides, on the binding of [14C]acetylated glycopeptides to columns of immobilized concanavalin A (Con A), Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin-120 (RCA-120) was investigated. The presence of this \"bisecting\" GlcNAc group caused significant inhibition of the binding to ConA-agarose of biantennary complex glycopeptides in which the two branches are terminated at their nonreducing ends by two GlcNAc groups, or by a Gal and a GlcNAc group, or by two Gal groups, or by a Man and a GlcNAc group. Binding of biantennary, complex glycopeptides to E-PHA-agarose required a \"bisecting\" GlcNAc group, a Gal group at the nonreducing terminus of the alpha-D-Man-p-(1----6) branch, and a terminal or internal GlcNAc residue linked beta-(1----2) to the alpha-D-Manp-(1----3) branch. Binding to RCA-120-agarose occurred only when at least one nonreducing terminal Gal group was present, and increased as the proportion of terminal Gal groups increased; the presence of a \"bisecting\" GlcNAc group caused either enhancement or inhibition of these binding patterns. It is concluded that a \"bisecting\" GlcNAc group affects the binding of glycopeptides to all three lectin columns."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":130,"end":148},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":180,"end":196},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":526,"end":544},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":576,"end":592},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3885"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3988"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3885"},{"id":"A4","pred":"db_id","subj":"T4","obj":"3988"}],"text":"The effect of a \"bisecting\" N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-120) immobilized on agarose.\nThe effect of a \"bisecting\" 2-acetamido-2-deoxy-beta-D-glucopyranosyl group, linked (1----4) to the beta-D-mannopyranosyl group of asparagine-linked complex and hybrid oligosaccharides, on the binding of [14C]acetylated glycopeptides to columns of immobilized concanavalin A (Con A), Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin-120 (RCA-120) was investigated. The presence of this \"bisecting\" GlcNAc group caused significant inhibition of the binding to ConA-agarose of biantennary complex glycopeptides in which the two branches are terminated at their nonreducing ends by two GlcNAc groups, or by a Gal and a GlcNAc group, or by two Gal groups, or by a Man and a GlcNAc group. Binding of biantennary, complex glycopeptides to E-PHA-agarose required a \"bisecting\" GlcNAc group, a Gal group at the nonreducing terminus of the alpha-D-Man-p-(1----6) branch, and a terminal or internal GlcNAc residue linked beta-(1----2) to the alpha-D-Manp-(1----3) branch. Binding to RCA-120-agarose occurred only when at least one nonreducing terminal Gal group was present, and increased as the proportion of terminal Gal groups increased; the presence of a \"bisecting\" GlcNAc group caused either enhancement or inhibition of these binding patterns. It is concluded that a \"bisecting\" GlcNAc group affects the binding of glycopeptides to all three lectin columns."}