| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-132 |
Sentence |
denotes |
Characterization of the substrate specificity of alpha1,3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides. |
| T1 |
0-132 |
Sentence |
denotes |
Characterization of the substrate specificity of alpha1,3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides. |
| T1 |
0-132 |
Sentence |
denotes |
Characterization of the substrate specificity of alpha1,3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides. |
| TextSentencer_T2 |
133-342 |
Sentence |
denotes |
alpha1,3galactosyltransferase (alpha1,3GalT) catalyzes the synthesis of a range of glycoconjugates containing the Galalpha1,3Gal epitope which is recognized by the naturally occurring human antibody, anti-Gal. |
| T2 |
133-342 |
Sentence |
denotes |
alpha1,3galactosyltransferase (alpha1,3GalT) catalyzes the synthesis of a range of glycoconjugates containing the Galalpha1,3Gal epitope which is recognized by the naturally occurring human antibody, anti-Gal. |
| T2 |
133-524 |
Sentence |
denotes |
alpha1,3galactosyltransferase (alpha1,3GalT) catalyzes the synthesis of a range of glycoconjugates containing the Galalpha1,3Gal epitope which is recognized by the naturally occurring human antibody, anti-Gal. This enzyme may be a useful synthetic tool to produce a range of compounds to further investigate the binding site of anti-Gal and other proteins with a Galalpha1,3Gal binding site. |
| TextSentencer_T3 |
343-524 |
Sentence |
denotes |
This enzyme may be a useful synthetic tool to produce a range of compounds to further investigate the binding site of anti-Gal and other proteins with a Galalpha1,3Gal binding site. |
| T3 |
343-524 |
Sentence |
denotes |
This enzyme may be a useful synthetic tool to produce a range of compounds to further investigate the binding site of anti-Gal and other proteins with a Galalpha1,3Gal binding site. |
| TextSentencer_T4 |
525-627 |
Sentence |
denotes |
Thus, the enzyme has been probed with a series of type 2 disaccharide-C8(Galbeta1-4GlcNAc-C8) analogs. |
| T3 |
525-627 |
Sentence |
denotes |
Thus, the enzyme has been probed with a series of type 2 disaccharide-C8(Galbeta1-4GlcNAc-C8) analogs. |
| T4 |
525-627 |
Sentence |
denotes |
Thus, the enzyme has been probed with a series of type 2 disaccharide-C8(Galbeta1-4GlcNAc-C8) analogs. |
| TextSentencer_T5 |
628-804 |
Sentence |
denotes |
The enzyme tolerated acceptors with modifications at C2 and C3 of the N-acetylglucosamine residue, producing a family of compounds with a nonreducing alpha1,3 linked galactose. |
| T4 |
628-804 |
Sentence |
denotes |
The enzyme tolerated acceptors with modifications at C2 and C3 of the N-acetylglucosamine residue, producing a family of compounds with a nonreducing alpha1,3 linked galactose. |
| T5 |
628-804 |
Sentence |
denotes |
The enzyme tolerated acceptors with modifications at C2 and C3 of the N-acetylglucosamine residue, producing a family of compounds with a nonreducing alpha1,3 linked galactose. |
| TextSentencer_T6 |
805-876 |
Sentence |
denotes |
Compounds that did not serve as acceptors were evaluated as inhibitors. |
| T5 |
805-876 |
Sentence |
denotes |
Compounds that did not serve as acceptors were evaluated as inhibitors. |
| T6 |
805-876 |
Sentence |
denotes |
Compounds that did not serve as acceptors were evaluated as inhibitors. |
| TextSentencer_T7 |
877-1038 |
Sentence |
denotes |
Interestingly, the type 1 disaccharide-C8, Galbeta1-3GlcNAc-C8, was a good inhibitor of the enzyme (Ki = 270 microM vs. Km = 190 microM for Galbeta1-4GlcNAc-C8). |
| T6 |
877-1038 |
Sentence |
denotes |
Interestingly, the type 1 disaccharide-C8, Galbeta1-3GlcNAc-C8, was a good inhibitor of the enzyme (Ki = 270 microM vs. Km = 190 microM for Galbeta1-4GlcNAc-C8). |
| T7 |
877-1038 |
Sentence |
denotes |
Interestingly, the type 1 disaccharide-C8, Galbeta1-3GlcNAc-C8, was a good inhibitor of the enzyme (Ki = 270 microM vs. Km = 190 microM for Galbeta1-4GlcNAc-C8). |
| TextSentencer_T8 |
1039-1431 |
Sentence |
denotes |
A potential photoprobe, based on a modified type 2 disaccharide (octyl 3-amino-3-deoxy-3-N-(2-diazo-3, 3, 3-trifluoropropionyl-beta-D-galactopyranosyl-(1, 4)-2-acetamindo-2-deoxy-beta-D-glycopyranoside, (DTFP-LacNAc-C8)), was evaluated as an inhibitor of alpha1,3GalT. alpha1,3GalT bound DTFP-LacNAc-C8 with an affinity (Ki = 300 microM) similar to that displayed by the enzyme for LacNAc-C8. |
| T7 |
1039-1431 |
Sentence |
denotes |
A potential photoprobe, based on a modified type 2 disaccharide (octyl 3-amino-3-deoxy-3-N-(2-diazo-3, 3, 3-trifluoropropionyl-beta-D-galactopyranosyl-(1, 4)-2-acetamindo-2-deoxy-beta-D-glycopyranoside, (DTFP-LacNAc-C8)), was evaluated as an inhibitor of alpha1,3GalT. alpha1,3GalT bound DTFP-LacNAc-C8 with an affinity (Ki = 300 microM) similar to that displayed by the enzyme for LacNAc-C8. |
| T8 |
1039-1431 |
Sentence |
denotes |
A potential photoprobe, based on a modified type 2 disaccharide (octyl 3-amino-3-deoxy-3-N-(2-diazo-3, 3, 3-trifluoropropionyl-beta-D-galactopyranosyl-(1, 4)-2-acetamindo-2-deoxy-beta-D-glycopyranoside, (DTFP-LacNAc-C8)), was evaluated as an inhibitor of alpha1,3GalT. alpha1,3GalT bound DTFP-LacNAc-C8 with an affinity (Ki = 300 microM) similar to that displayed by the enzyme for LacNAc-C8. |
| TextSentencer_T9 |
1432-1547 |
Sentence |
denotes |
Additional studies were done to determine the enzyme's ability to transfer a range of sugars from UDP-sugar donors. |
| T8 |
1432-1547 |
Sentence |
denotes |
Additional studies were done to determine the enzyme's ability to transfer a range of sugars from UDP-sugar donors. |
| T9 |
1432-1547 |
Sentence |
denotes |
Additional studies were done to determine the enzyme's ability to transfer a range of sugars from UDP-sugar donors. |
| TextSentencer_T10 |
1548-1649 |
Sentence |
denotes |
The results of these experiments demonstrated that alpha1,3GalT has a strict specificity for UDP-Gal. |
| T10 |
1548-1649 |
Sentence |
denotes |
The results of these experiments demonstrated that alpha1,3GalT has a strict specificity for UDP-Gal. |
| T9 |
1548-1824 |
Sentence |
denotes |
The results of these experiments demonstrated that alpha1,3GalT has a strict specificity for UDP-Gal. Finally, inactivation studies with various amino acid modifiers were done to obtain information on the importance of different types of amino acids for alpha1,3GalT activity. |
| TextSentencer_T11 |
1650-1824 |
Sentence |
denotes |
Finally, inactivation studies with various amino acid modifiers were done to obtain information on the importance of different types of amino acids for alpha1,3GalT activity. |
| T11 |
1650-1824 |
Sentence |
denotes |
Finally, inactivation studies with various amino acid modifiers were done to obtain information on the importance of different types of amino acids for alpha1,3GalT activity. |