PubMed:1933954 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":50},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":51,"end":132},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":133,"end":333},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":334,"end":351},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":352,"end":354},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":355,"end":369},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":370,"end":413},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":414,"end":784},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":785,"end":953},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":954,"end":1035},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1036,"end":1115},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1116,"end":1231},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1232,"end":1410},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":1411,"end":1582},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":50},"obj":"Sentence"},{"id":"T2","span":{"begin":51,"end":132},"obj":"Sentence"},{"id":"T3","span":{"begin":133,"end":333},"obj":"Sentence"},{"id":"T4","span":{"begin":334,"end":351},"obj":"Sentence"},{"id":"T5","span":{"begin":352,"end":354},"obj":"Sentence"},{"id":"T6","span":{"begin":355,"end":369},"obj":"Sentence"},{"id":"T7","span":{"begin":370,"end":413},"obj":"Sentence"},{"id":"T8","span":{"begin":414,"end":784},"obj":"Sentence"},{"id":"T9","span":{"begin":785,"end":953},"obj":"Sentence"},{"id":"T10","span":{"begin":954,"end":1035},"obj":"Sentence"},{"id":"T11","span":{"begin":1036,"end":1115},"obj":"Sentence"},{"id":"T12","span":{"begin":1116,"end":1231},"obj":"Sentence"},{"id":"T13","span":{"begin":1232,"end":1410},"obj":"Sentence"},{"id":"T14","span":{"begin":1411,"end":1582},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin.\nCertain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C.F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":113,"end":120},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":653,"end":660},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":662,"end":673},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3847"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3847"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3847"}],"text":"Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin.\nCertain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C.F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":349,"end":353},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0001658"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin.\nCertain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C.F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA."}