| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-134 |
Sentence |
denotes |
Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1-->6fucosyltransferase from human blood platelets. |
| T1 |
0-134 |
Sentence |
denotes |
Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1-->6fucosyltransferase from human blood platelets. |
| TextSentencer_T2 |
135-304 |
Sentence |
denotes |
c-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. |
| T2 |
135-304 |
Sentence |
denotes |
c-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. |
| TextSentencer_T3 |
305-523 |
Sentence |
denotes |
The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. |
| T3 |
305-523 |
Sentence |
denotes |
The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. |
| TextSentencer_T4 |
524-795 |
Sentence |
denotes |
The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. |
| T4 |
524-795 |
Sentence |
denotes |
The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. |
| TextSentencer_T5 |
796-998 |
Sentence |
denotes |
Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. |
| T5 |
796-998 |
Sentence |
denotes |
Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. |
| TextSentencer_T6 |
999-1082 |
Sentence |
denotes |
On the other hand the tetraantennary oligosaccharide was not a preferred substrate. |
| T6 |
999-1082 |
Sentence |
denotes |
On the other hand the tetraantennary oligosaccharide was not a preferred substrate. |
| TextSentencer_T7 |
1083-1209 |
Sentence |
denotes |
The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. |
| T7 |
1083-1209 |
Sentence |
denotes |
The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. |
| TextSentencer_T8 |
1210-1247 |
Sentence |
denotes |
The optimum pH of the enzyme was 6.0. |
| T8 |
1210-1247 |
Sentence |
denotes |
The optimum pH of the enzyme was 6.0. |
| TextSentencer_T9 |
1248-1331 |
Sentence |
denotes |
The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. |
| T9 |
1248-1331 |
Sentence |
denotes |
The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. |
| TextSentencer_T10 |
1332-1438 |
Sentence |
denotes |
Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity. |
| T10 |
1332-1438 |
Sentence |
denotes |
Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity. |