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. |
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. |
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. |
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. |
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. |
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. |
TextSentencer_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. |
T1 |
0-114 |
Sentence |
denotes |
Affinity of four immobilized Erythrina lectins toward various N-linked glycopeptides and related oligosaccharides. |
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. |
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. |
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. |
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. |
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. |
T7 |
1087-1212 |
Sentence |
denotes |
Surprisingly, the affinity of the lectins for the oligosaccharides tested is higher than for the corresponding 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. |