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PubMed:3768898 JSONTXT 23 Projects

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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-114 Sentence denotes Affinity of four immobilized Erythrina lectins toward various N-linked glycopeptides and related oligosaccharides.
T1 0-114 Sentence denotes Affinity of four immobilized Erythrina lectins toward various N-linked glycopeptides and related oligosaccharides.
TextSentencer_T2 115-280 Sentence denotes The behavior of N-acetyllactosamine-type oligosaccharides and glycopeptides on columns of four different Erythrina agglutinins immobilized on Sepharose was examined.
T2 115-280 Sentence denotes The behavior of N-acetyllactosamine-type oligosaccharides and glycopeptides on columns of four different Erythrina agglutinins immobilized on Sepharose was examined.
TextSentencer_T3 281-533 Sentence denotes The sugar-binding specificity of the four lectins is very similar and is directed toward unmasked N-acetyllactosamine sequences, the main difference between the four lectins being the relative strength of interaction of the lectins with a given glycan.
T3 281-533 Sentence denotes The sugar-binding specificity of the four lectins is very similar and is directed toward unmasked N-acetyllactosamine sequences, the main difference between the four lectins being the relative strength of interaction of the lectins with a given glycan.
TextSentencer_T4 534-712 Sentence denotes Substitution of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose completely abolishes the affinity of the lectins for the saccharides.
T4 534-712 Sentence denotes Substitution of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose completely abolishes the affinity of the lectins for the saccharides.
TextSentencer_T5 713-878 Sentence denotes The presence of one or several alpha-Fuc-(1----3)-GlcNAc groups decreases or completely inhibits the interaction between the glycopeptides and the Erythrina lectins.
T5 713-878 Sentence denotes The presence of one or several alpha-Fuc-(1----3)-GlcNAc groups decreases or completely inhibits the interaction between the glycopeptides and the Erythrina lectins.
TextSentencer_T6 879-1086 Sentence denotes Substitution of the beta-mannose residue by an additional bisecting beta-(1----4)-N-acetylglucosamine residue decreases the affinity of the lectins for these structures as compared to the unsubstituted ones.
T6 879-1086 Sentence denotes Substitution of the beta-mannose residue by an additional bisecting beta-(1----4)-N-acetylglucosamine residue decreases the affinity of the lectins for these structures as compared to the unsubstituted ones.
TextSentencer_T7 1087-1212 Sentence denotes Surprisingly, the affinity of the lectins for the oligosaccharides tested is higher than for the corresponding glycopeptides.
T7 1087-1212 Sentence denotes Surprisingly, the affinity of the lectins for the oligosaccharides tested is higher than for the corresponding glycopeptides.
TextSentencer_T8 1213-1486 Sentence denotes Our findings show that, after careful calibration with well-defined oligosaccharides and glycopeptides, the immobilized Erythrina agglutinin-Sepharose columns provide valuable tools for the fractionation of N-acetyllactosamine-containing oligosaccharides and glycopeptides.
T8 1213-1486 Sentence denotes Our findings show that, after careful calibration with well-defined oligosaccharides and glycopeptides, the immobilized Erythrina agglutinin-Sepharose columns provide valuable tools for the fractionation of N-acetyllactosamine-containing oligosaccharides and glycopeptides.