PubMed:7795413 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1551,"end":1562},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T3","span":{"begin":337,"end":342},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T4","span":{"begin":337,"end":342},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T5","span":{"begin":573,"end":578},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1551,"end":1562},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":272},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":273,"end":687},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":688,"end":1002},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":1003,"end":1146},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1147,"end":1305},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1306,"end":1687},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":272},"obj":"Sentence"},{"id":"T2","span":{"begin":273,"end":687},"obj":"Sentence"},{"id":"T3","span":{"begin":688,"end":1002},"obj":"Sentence"},{"id":"T4","span":{"begin":1003,"end":1146},"obj":"Sentence"},{"id":"T5","span":{"begin":1147,"end":1305},"obj":"Sentence"},{"id":"T6","span":{"begin":1306,"end":1687},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":101,"end":107},"obj":"Glycan"},{"id":"T2","span":{"begin":387,"end":393},"obj":"Glycan"},{"id":"T3","span":{"begin":1202,"end":1208},"obj":"Glycan"},{"id":"T4","span":{"begin":1577,"end":1583},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":478,"end":495},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":497,"end":500},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":503,"end":516},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":518,"end":521},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":527,"end":540},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":885,"end":888},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":935,"end":938},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1050,"end":1053},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1134,"end":1137},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":1301,"end":1304},"obj":"OrganismTaxon"},{"id":"T11","span":{"begin":1517,"end":1520},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":1632,"end":1635},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"5341"},{"id":"A2","pred":"db_id","subj":"T2","obj":"5341"},{"id":"A3","pred":"db_id","subj":"T3","obj":"6536"},{"id":"A4","pred":"db_id","subj":"T4","obj":"6536"},{"id":"A5","pred":"db_id","subj":"T5","obj":"3911"},{"id":"A6","pred":"db_id","subj":"T6","obj":"5341"},{"id":"A7","pred":"db_id","subj":"T7","obj":"6536"},{"id":"A8","pred":"db_id","subj":"T8","obj":"6536"},{"id":"A9","pred":"db_id","subj":"T9","obj":"5341"},{"id":"A10","pred":"db_id","subj":"T10","obj":"5341"},{"id":"A11","pred":"db_id","subj":"T11","obj":"5341"},{"id":"A12","pred":"db_id","subj":"T12","obj":"6536"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":149,"end":154},"obj":"Body_part"},{"id":"T2","span":{"begin":337,"end":342},"obj":"Body_part"},{"id":"T3","span":{"begin":503,"end":508},"obj":"Body_part"},{"id":"T4","span":{"begin":564,"end":578},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002488"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002366"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":149,"end":154},"obj":"Body_part"},{"id":"T3","span":{"begin":337,"end":342},"obj":"Body_part"},{"id":"T5","span":{"begin":573,"end":578},"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"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A4","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":272},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":273,"end":687},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":688,"end":1002},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":1003,"end":1146},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1147,"end":1305},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1306,"end":1687},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":272},"obj":"Sentence"},{"id":"T2","span":{"begin":273,"end":687},"obj":"Sentence"},{"id":"T3","span":{"begin":688,"end":1002},"obj":"Sentence"},{"id":"T4","span":{"begin":1003,"end":1146},"obj":"Sentence"},{"id":"T5","span":{"begin":1147,"end":1305},"obj":"Sentence"},{"id":"T6","span":{"begin":1306,"end":1687},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":272},"obj":"Sentence"},{"id":"T2","span":{"begin":273,"end":687},"obj":"Sentence"},{"id":"T3","span":{"begin":688,"end":1002},"obj":"Sentence"},{"id":"T4","span":{"begin":1003,"end":1146},"obj":"Sentence"},{"id":"T5","span":{"begin":1147,"end":1305},"obj":"Sentence"},{"id":"T6","span":{"begin":1306,"end":1687},"obj":"Sentence"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":101,"end":107},"obj":"Glycan"},{"id":"T2","span":{"begin":387,"end":393},"obj":"Glycan"},{"id":"T3","span":{"begin":1202,"end":1208},"obj":"Glycan"},{"id":"T4","span":{"begin":1577,"end":1583},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"GlyCosmos15-Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":472,"end":475},"obj":"Lectin"},{"id":"T2","span":{"begin":497,"end":500},"obj":"Lectin"},{"id":"T3","span":{"begin":518,"end":521},"obj":"Lectin"},{"id":"T4","span":{"begin":545,"end":548},"obj":"Lectin"},{"id":"T5","span":{"begin":878,"end":881},"obj":"Lectin"},{"id":"T6","span":{"begin":885,"end":888},"obj":"Lectin"},{"id":"T7","span":{"begin":935,"end":938},"obj":"Lectin"},{"id":"T8","span":{"begin":943,"end":946},"obj":"Lectin"},{"id":"T9","span":{"begin":1050,"end":1053},"obj":"Lectin"},{"id":"T10","span":{"begin":1057,"end":1060},"obj":"Lectin"},{"id":"T11","span":{"begin":1126,"end":1129},"obj":"Lectin"},{"id":"T12","span":{"begin":1134,"end":1137},"obj":"Lectin"},{"id":"T13","span":{"begin":1259,"end":1262},"obj":"Lectin"},{"id":"T14","span":{"begin":1301,"end":1304},"obj":"Lectin"},{"id":"T15","span":{"begin":1452,"end":1455},"obj":"Lectin"},{"id":"T16","span":{"begin":1517,"end":1520},"obj":"Lectin"},{"id":"T17","span":{"begin":1632,"end":1635},"obj":"Lectin"},{"id":"T18","span":{"begin":1640,"end":1643},"obj":"Lectin"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"GL_003655"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"GL_001756"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"GL_005054"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"GL_001760"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"GL_003655"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"GL_001756"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"GL_005054"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"GL_001760"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"GL_005054"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"GL_001760"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"GL_003655"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"GL_001756"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"GL_003655"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"GL_001756"},{"id":"A15","pred":"glycosmos_id","subj":"T15","obj":"GL_003655"},{"id":"A16","pred":"glycosmos_id","subj":"T16","obj":"GL_001756"},{"id":"A17","pred":"glycosmos_id","subj":"T17","obj":"GL_005054"},{"id":"A18","pred":"glycosmos_id","subj":"T18","obj":"GL_001760"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":478,"end":495},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":497,"end":500},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":503,"end":516},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":518,"end":521},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":527,"end":540},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":885,"end":888},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":935,"end":938},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1050,"end":1053},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1134,"end":1137},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":1301,"end":1304},"obj":"OrganismTaxon"},{"id":"T11","span":{"begin":1517,"end":1520},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":1632,"end":1635},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"5341"},{"id":"A2","pred":"db_id","subj":"T2","obj":"5341"},{"id":"A3","pred":"db_id","subj":"T3","obj":"6536"},{"id":"A4","pred":"db_id","subj":"T4","obj":"6536"},{"id":"A5","pred":"db_id","subj":"T5","obj":"3911"},{"id":"A6","pred":"db_id","subj":"T6","obj":"5341"},{"id":"A7","pred":"db_id","subj":"T7","obj":"6536"},{"id":"A8","pred":"db_id","subj":"T8","obj":"6536"},{"id":"A9","pred":"db_id","subj":"T9","obj":"5341"},{"id":"A10","pred":"db_id","subj":"T10","obj":"5341"},{"id":"A11","pred":"db_id","subj":"T11","obj":"5341"},{"id":"A12","pred":"db_id","subj":"T12","obj":"6536"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":149,"end":154},"obj":"Body_part"},{"id":"T2","span":{"begin":337,"end":342},"obj":"Body_part"},{"id":"T3","span":{"begin":503,"end":508},"obj":"Body_part"},{"id":"T4","span":{"begin":564,"end":578},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002488"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002366"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":149,"end":154},"obj":"Body_part"},{"id":"T3","span":{"begin":337,"end":342},"obj":"Body_part"},{"id":"T5","span":{"begin":573,"end":578},"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"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A4","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients.\nSialylated or sulfated derivatives and acrylamide copolymers of blood group T-(Gal beta 1,3GalNAc alpha-) and Tn-(GalNAc alpha) haptens were studied for their interaction with the lectins of peanut (PNA), Agaricus bisporus-(ABA), Helix pomatia-(HPA) and Vicia villosa B4-(VVA), using asialo Cowper's gland mucin (ACGM), which contains both T and Tn epitopes, as the coating substrate in enzyme linked lectin assay. Both T and Tn copolymers (-40 haptens) showed high affinity and strict specificity; although the T-copolymer at 0.05-0.07 microM concentration caused 50% inhibition of interaction of either PNA or ABA with ACGM, there was little inhibition of the HPA and VVA interactions even at over 100 times that concentration. The Tn-copolymer at 0.02-0.05 microM inhibited HPA or VVA interaction with ACGM by 50% but gave virtually no inhibition of PNA and ABA binding. Sialyl, sulfate or methyl group substitution on C-6 of GalNAc of the T-haptene did not prevent interaction with PNA but almost abolished interaction with ABA. In contrast, sialyl or sulfate group on C-6 and sulfate on C-3 of Gal in Gal beta 1,3GalNAc alpha- inhibited almost completely the interaction of PNA with ACGM but had only a slight effect on the interaction of ABA; C-6 substitution with either sialic acid or sulfate on GalNAc alpha- almost abolished the interaction of both HPA and VVA with ACGM.(ABSTRACT TRUNCATED AT 250 WORDS)"}