| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-136 |
Sentence |
denotes |
Flexibility in the donor substrate specificity of beta 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates. |
| T1 |
0-136 |
Sentence |
denotes |
Flexibility in the donor substrate specificity of beta 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates. |
| T1 |
0-136 |
Sentence |
denotes |
Flexibility in the donor substrate specificity of beta 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates. |
| TextSentencer_T2 |
137-375 |
Sentence |
denotes |
Biosynthetically, bovine N-acetylglucosamine beta 1,4-galactosyltransferase (GalT) catalyses the transfer of galactosyl residues from UDP-Gal to the 4-position of GlcNAc units, resulting in the production of N-acetyllactosamine sequences. |
| T2 |
137-375 |
Sentence |
denotes |
Biosynthetically, bovine N-acetylglucosamine beta 1,4-galactosyltransferase (GalT) catalyses the transfer of galactosyl residues from UDP-Gal to the 4-position of GlcNAc units, resulting in the production of N-acetyllactosamine sequences. |
| T2 |
137-375 |
Sentence |
denotes |
Biosynthetically, bovine N-acetylglucosamine beta 1,4-galactosyltransferase (GalT) catalyses the transfer of galactosyl residues from UDP-Gal to the 4-position of GlcNAc units, resulting in the production of N-acetyllactosamine sequences. |
| TextSentencer_T3 |
376-588 |
Sentence |
denotes |
UDP-Glc and UDP-GalNAc were also found to act as donors for this enzyme, allowing the preparation of beta Glc(1----4)-beta GlcNAc and beta GalNAc(1----4) beta GlcNAc terminating structures on the milligram scale. |
| T3 |
376-588 |
Sentence |
denotes |
UDP-Glc and UDP-GalNAc were also found to act as donors for this enzyme, allowing the preparation of beta Glc(1----4)-beta GlcNAc and beta GalNAc(1----4) beta GlcNAc terminating structures on the milligram scale. |
| T3 |
376-588 |
Sentence |
denotes |
UDP-Glc and UDP-GalNAc were also found to act as donors for this enzyme, allowing the preparation of beta Glc(1----4)-beta GlcNAc and beta GalNAc(1----4) beta GlcNAc terminating structures on the milligram scale. |
| TextSentencer_T4 |
589-803 |
Sentence |
denotes |
GalT could thus be used to add beta GalNAc to beta GlcNAc(1----2) alpha Man terminating structures, converting them to the beta GalNAc(1----4) beta GlcNAc(1----2) alpha Man sequences found on glycoprotein hormones. |
| T4 |
589-803 |
Sentence |
denotes |
GalT could thus be used to add beta GalNAc to beta GlcNAc(1----2) alpha Man terminating structures, converting them to the beta GalNAc(1----4) beta GlcNAc(1----2) alpha Man sequences found on glycoprotein hormones. |
| T4 |
589-803 |
Sentence |
denotes |
GalT could thus be used to add beta GalNAc to beta GlcNAc(1----2) alpha Man terminating structures, converting them to the beta GalNAc(1----4) beta GlcNAc(1----2) alpha Man sequences found on glycoprotein hormones. |
| TextSentencer_T5 |
804-902 |
Sentence |
denotes |
GalT did not transfer GlcNAc residues from UDP-GlcNAc, but it could utilize UDP-GlcNH2 as a donor. |
| T5 |
804-902 |
Sentence |
denotes |
GalT did not transfer GlcNAc residues from UDP-GlcNAc, but it could utilize UDP-GlcNH2 as a donor. |
| T5 |
804-902 |
Sentence |
denotes |
GalT did not transfer GlcNAc residues from UDP-GlcNAc, but it could utilize UDP-GlcNH2 as a donor. |
| TextSentencer_T6 |
903-1132 |
Sentence |
denotes |
Synthesis of beta GlcNAc(1----4) beta GlcNAc sequences could therefore be accomplished by transfer of GlcNH2 from its UDP derivative, followed by N-acetylation of the product amino-disaccharide using acetic anhydride in methanol. |
| T6 |
903-1132 |
Sentence |
denotes |
Synthesis of beta GlcNAc(1----4) beta GlcNAc sequences could therefore be accomplished by transfer of GlcNH2 from its UDP derivative, followed by N-acetylation of the product amino-disaccharide using acetic anhydride in methanol. |
| T6 |
903-1132 |
Sentence |
denotes |
Synthesis of beta GlcNAc(1----4) beta GlcNAc sequences could therefore be accomplished by transfer of GlcNH2 from its UDP derivative, followed by N-acetylation of the product amino-disaccharide using acetic anhydride in methanol. |
| TextSentencer_T7 |
1133-1259 |
Sentence |
denotes |
The products of the enzymatic reactions were characterized by 1H-NMR-spectroscopy and fast-atom bombardment mass spectrometry. |
| T7 |
1133-1259 |
Sentence |
denotes |
The products of the enzymatic reactions were characterized by 1H-NMR-spectroscopy and fast-atom bombardment mass spectrometry. |
| T7 |
1133-1259 |
Sentence |
denotes |
The products of the enzymatic reactions were characterized by 1H-NMR-spectroscopy and fast-atom bombardment mass spectrometry. |
| TextSentencer_T8 |
1260-1484 |
Sentence |
denotes |
This work expands the scope of the combined chemical-enzymatic synthesis of complex carbohydrates, using glycosyltransferases, to the production of oligosaccharides different from those for which these enzymes were designed. |
| T8 |
1260-1484 |
Sentence |
denotes |
This work expands the scope of the combined chemical-enzymatic synthesis of complex carbohydrates, using glycosyltransferases, to the production of oligosaccharides different from those for which these enzymes were designed. |
| T8 |
1260-1484 |
Sentence |
denotes |
This work expands the scope of the combined chemical-enzymatic synthesis of complex carbohydrates, using glycosyltransferases, to the production of oligosaccharides different from those for which these enzymes were designed. |
| TextSentencer_T9 |
1485-1578 |
Sentence |
denotes |
These unnatural reactions should find application in glycoprotein and glycolipid remodelling. |
| T9 |
1485-1578 |
Sentence |
denotes |
These unnatural reactions should find application in glycoprotein and glycolipid remodelling. |
| T9 |
1485-1578 |
Sentence |
denotes |
These unnatural reactions should find application in glycoprotein and glycolipid remodelling. |