| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-107 |
Sentence |
denotes |
Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1. |
| T1 |
0-107 |
Sentence |
denotes |
Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1. |
| T1 |
0-107 |
Sentence |
denotes |
Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1. |
| TextSentencer_T2 |
108-295 |
Sentence |
denotes |
As part of a study of protein-carbohydrate interactions, linear N-acetyl-polyllactosamines [Galbeta1,4GlcNAcbeta1,3]nwere synthesized at the 10-100 micromol scale using enzymatic methods. |
| T2 |
108-295 |
Sentence |
denotes |
As part of a study of protein-carbohydrate interactions, linear N-acetyl-polyllactosamines [Galbeta1,4GlcNAcbeta1,3]nwere synthesized at the 10-100 micromol scale using enzymatic methods. |
| T2 |
108-295 |
Sentence |
denotes |
As part of a study of protein-carbohydrate interactions, linear N-acetyl-polyllactosamines [Galbeta1,4GlcNAcbeta1,3]nwere synthesized at the 10-100 micromol scale using enzymatic methods. |
| TextSentencer_T3 |
296-543 |
Sentence |
denotes |
The methods described also provided specifically [1-13C]-galactose-labeled tetra- and hexasaccharides ([1-13C]-Galbeta1,4GlcNAcbeta1,3Galbeta1,4Glc and Galbeta1, 4GlcNAcbeta1,3[1-13C]Galbeta1,4GlcNAcbeta1,3Galbeta 1,4Glc) suitable for NMR studies. |
| T3 |
296-543 |
Sentence |
denotes |
The methods described also provided specifically [1-13C]-galactose-labeled tetra- and hexasaccharides ([1-13C]-Galbeta1,4GlcNAcbeta1,3Galbeta1,4Glc and Galbeta1, 4GlcNAcbeta1,3[1-13C]Galbeta1,4GlcNAcbeta1,3Galbeta 1,4Glc) suitable for NMR studies. |
| T3 |
296-543 |
Sentence |
denotes |
The methods described also provided specifically [1-13C]-galactose-labeled tetra- and hexasaccharides ([1-13C]-Galbeta1,4GlcNAcbeta1,3Galbeta1,4Glc and Galbeta1, 4GlcNAcbeta1,3[1-13C]Galbeta1,4GlcNAcbeta1,3Galbeta 1,4Glc) suitable for NMR studies. |
| TextSentencer_T4 |
544-653 |
Sentence |
denotes |
Two series of oligosaccharides were produced, with either glucose or N-acetlyglucosamine at the reducing end. |
| T4 |
544-653 |
Sentence |
denotes |
Two series of oligosaccharides were produced, with either glucose or N-acetlyglucosamine at the reducing end. |
| T4 |
544-653 |
Sentence |
denotes |
Two series of oligosaccharides were produced, with either glucose or N-acetlyglucosamine at the reducing end. |
| TextSentencer_T5 |
654-852 |
Sentence |
denotes |
In both cases, large amounts of starting primer were available from human milk oligosaccharides (trisaccharide primer GlcNAcbeta1,3Galbeta1, 4Glc) or via transglycosylation from N-acetyllactosamine. |
| T5 |
654-852 |
Sentence |
denotes |
In both cases, large amounts of starting primer were available from human milk oligosaccharides (trisaccharide primer GlcNAcbeta1,3Galbeta1, 4Glc) or via transglycosylation from N-acetyllactosamine. |
| T5 |
654-852 |
Sentence |
denotes |
In both cases, large amounts of starting primer were available from human milk oligosaccharides (trisaccharide primer GlcNAcbeta1,3Galbeta1, 4Glc) or via transglycosylation from N-acetyllactosamine. |
| TextSentencer_T6 |
853-1046 |
Sentence |
denotes |
Partially purified and immobilized glycosyltransferases, such as bovine milk beta1,4 galactosyltransferase and human serum beta1,3 N- acetylglucosaminyltransferase, were used for the synthesis. |
| T6 |
853-1046 |
Sentence |
denotes |
Partially purified and immobilized glycosyltransferases, such as bovine milk beta1,4 galactosyltransferase and human serum beta1,3 N- acetylglucosaminyltransferase, were used for the synthesis. |
| T6 |
853-1046 |
Sentence |
denotes |
Partially purified and immobilized glycosyltransferases, such as bovine milk beta1,4 galactosyltransferase and human serum beta1,3 N- acetylglucosaminyltransferase, were used for the synthesis. |
| TextSentencer_T7 |
1047-1161 |
Sentence |
denotes |
All the oligo-saccharide products were characterized by1H and13C NMR spectroscopy and MALDI-TOF mass spectrometry. |
| T7 |
1047-1161 |
Sentence |
denotes |
All the oligo-saccharide products were characterized by1H and13C NMR spectroscopy and MALDI-TOF mass spectrometry. |
| T7 |
1047-1161 |
Sentence |
denotes |
All the oligo-saccharide products were characterized by1H and13C NMR spectroscopy and MALDI-TOF mass spectrometry. |
| TextSentencer_T8 |
1162-1337 |
Sentence |
denotes |
The target molecules were then used to study their interactions with recombinant galectin-1, and initial1H NMR spectroscopic results are presented to illustrate this approach. |
| T8 |
1162-1337 |
Sentence |
denotes |
The target molecules were then used to study their interactions with recombinant galectin-1, and initial1H NMR spectroscopic results are presented to illustrate this approach. |
| T8 |
1162-1337 |
Sentence |
denotes |
The target molecules were then used to study their interactions with recombinant galectin-1, and initial1H NMR spectroscopic results are presented to illustrate this approach. |
| TextSentencer_T9 |
1338-1522 |
Sentence |
denotes |
These results indicate that, for oligomers containing up to eight sugars, the principal interaction of the binding site of galectin-1 is with the terminal N-acetyllactosamine residues. |
| T9 |
1338-1522 |
Sentence |
denotes |
These results indicate that, for oligomers containing up to eight sugars, the principal interaction of the binding site of galectin-1 is with the terminal N-acetyllactosamine residues. |
| T9 |
1338-1522 |
Sentence |
denotes |
These results indicate that, for oligomers containing up to eight sugars, the principal interaction of the binding site of galectin-1 is with the terminal N-acetyllactosamine residues. |