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GlyCosmos15-Species

{"project":"GlyCosmos15-Species","denotations":[{"id":"2","span":{"begin":30,"end":63},"obj":"Species"},{"id":"37","span":{"begin":204,"end":237},"obj":"Species"},{"id":"38","span":{"begin":239,"end":243},"obj":"Species"},{"id":"40","span":{"begin":320,"end":325},"obj":"Species"},{"id":"42","span":{"begin":420,"end":425},"obj":"Species"},{"id":"46","span":{"begin":563,"end":568},"obj":"Species"},{"id":"52","span":{"begin":816,"end":821},"obj":"Species"},{"id":"53","span":{"begin":851,"end":856},"obj":"Species"},{"id":"67","span":{"begin":1735,"end":1739},"obj":"Species"}],"attributes":[{"id":"A40","pred":"db_id","subj":"40","obj":"9606"},{"id":"A42","pred":"db_id","subj":"42","obj":"9606"},{"id":"A46","pred":"db_id","subj":"46","obj":"9606"},{"id":"A52","pred":"db_id","subj":"52","obj":"9606"},{"id":"A53","pred":"db_id","subj":"53","obj":"9606"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

GlyCosmos6-Glycan-Motif-Image

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":98,"end":103},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":98,"end":103},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T3","span":{"begin":130,"end":135},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T4","span":{"begin":130,"end":135},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T5","span":{"begin":350,"end":355},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T6","span":{"begin":350,"end":355},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T7","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T8","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T9","span":{"begin":569,"end":574},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T10","span":{"begin":569,"end":574},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T11","span":{"begin":599,"end":605},"obj":"http://purl.obolibrary.org/obo/MAT_0000444"},{"id":"T12","span":{"begin":645,"end":650},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T13","span":{"begin":645,"end":650},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T14","span":{"begin":822,"end":827},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T15","span":{"begin":822,"end":827},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T16","span":{"begin":857,"end":862},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T17","span":{"begin":857,"end":862},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":184},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":185,"end":349},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":350,"end":629},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":630,"end":779},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":780,"end":958},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":959,"end":1411},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1412,"end":1659},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1660,"end":2073},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":184},"obj":"Sentence"},{"id":"T2","span":{"begin":185,"end":349},"obj":"Sentence"},{"id":"T3","span":{"begin":350,"end":629},"obj":"Sentence"},{"id":"T4","span":{"begin":630,"end":779},"obj":"Sentence"},{"id":"T5","span":{"begin":780,"end":958},"obj":"Sentence"},{"id":"T6","span":{"begin":959,"end":1411},"obj":"Sentence"},{"id":"T7","span":{"begin":1412,"end":1659},"obj":"Sentence"},{"id":"T8","span":{"begin":1660,"end":2073},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

GlyCosmos6-Glycan-Motif-Structure

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":130,"end":143},"obj":"Glycan"},{"id":"T2","span":{"begin":569,"end":582},"obj":"Glycan"},{"id":"T3","span":{"begin":857,"end":870},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00066MO"},{"id":"A4","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00066MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00066MO"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00066MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00066MO"},{"id":"A6","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00066MO"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":239,"end":243},"obj":"Disease"},{"id":"T2","span":{"begin":332,"end":337},"obj":"Disease"},{"id":"T3","span":{"begin":426,"end":438},"obj":"Disease"},{"id":"T4","span":{"begin":535,"end":539},"obj":"Disease"},{"id":"T5","span":{"begin":610,"end":622},"obj":"Disease"},{"id":"T6","span":{"begin":742,"end":747},"obj":"Disease"},{"id":"T7","span":{"begin":761,"end":765},"obj":"Disease"},{"id":"T8","span":{"begin":789,"end":793},"obj":"Disease"},{"id":"T9","span":{"begin":1735,"end":1739},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0015085"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0009796"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0003282"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0015085"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0003282"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0009796"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0015085"},{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0015085"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MONDO_0015085"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

HP-phenotype

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":426,"end":438},"obj":"Phenotype"},{"id":"T2","span":{"begin":610,"end":622},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0000138"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0000138"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

GlyCosmos15-HP

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":426,"end":438},"obj":"Phenotype"},{"id":"T2","span":{"begin":610,"end":622},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0000138"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0000138"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":184},"obj":"Sentence"},{"id":"T2","span":{"begin":185,"end":349},"obj":"Sentence"},{"id":"T3","span":{"begin":350,"end":629},"obj":"Sentence"},{"id":"T4","span":{"begin":630,"end":779},"obj":"Sentence"},{"id":"T5","span":{"begin":780,"end":958},"obj":"Sentence"},{"id":"T6","span":{"begin":959,"end":1659},"obj":"Sentence"},{"id":"T7","span":{"begin":1660,"end":2073},"obj":"Sentence"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

GlyCosmos15-MONDO

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":426,"end":438},"obj":"Disease"},{"id":"T2","span":{"begin":610,"end":622},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0003282"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0003282"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":420,"end":425},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":563,"end":568},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":816,"end":821},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":851,"end":856},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":98,"end":103},"obj":"Body_part"},{"id":"T2","span":{"begin":130,"end":135},"obj":"Body_part"},{"id":"T3","span":{"begin":350,"end":355},"obj":"Body_part"},{"id":"T4","span":{"begin":395,"end":410},"obj":"Body_part"},{"id":"T5","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T6","span":{"begin":569,"end":574},"obj":"Body_part"},{"id":"T7","span":{"begin":599,"end":605},"obj":"Body_part"},{"id":"T8","span":{"begin":623,"end":628},"obj":"Body_part"},{"id":"T9","span":{"begin":645,"end":650},"obj":"Body_part"},{"id":"T10","span":{"begin":822,"end":827},"obj":"Body_part"},{"id":"T11","span":{"begin":857,"end":862},"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_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001199"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0001836"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0006314"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides.\nThe specificity of Bandeiraea simplicifolia lectin I (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active aligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl alpha-D-GalNAcp, D-GalNAcp, and an A active pentasaccharide ARL 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains alpha-D-GalNAcp-(1 leads to 3)-2-acetamido-2-deoxy-D-galactitol and p-nitrophenyl alpha-D-GalNAcp, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, alpha-linked D-Galp. The most potent inhibitors of this group were p-nitrophenyl alpha-D-Galp, alpha-D-Galp-(1 leads to 3)-D-Galp, alpha-D-Galp-(1 leads to 6)-D-Glcp, and methyl alpha-D-Galp, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for alpha-linked, terminal, nonreducing D-GalNAcp, but it also reacts with alpha-linked, terminal, nonreducing D-Galp, whereas subunit B tends to be more specific for terminal, nonreducing, alpha-linked D-Galp."}

Anatomy-MAT