Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-127 |
Sentence |
denotes |
The putative heparin-specific N-acetylglucosaminyl N-Deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells. |
T1 |
0-127 |
Sentence |
denotes |
The putative heparin-specific N-acetylglucosaminyl N-Deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells. |
T2 |
128-435 |
Sentence |
denotes |
N-Deacetylation and N-sulfation of N-acetylglucosamine of heparin and heparan sulfate are hypothesized to be mediated by different tissue-specific N-acetylglucosaminyl N-deacetylases/N-sulfotransferases, which in turn lead to the higher L-iduronic acid and sulfate content of heparin versus heparan sulfate. |
T2 |
128-435 |
Sentence |
denotes |
N-Deacetylation and N-sulfation of N-acetylglucosamine of heparin and heparan sulfate are hypothesized to be mediated by different tissue-specific N-acetylglucosaminyl N-deacetylases/N-sulfotransferases, which in turn lead to the higher L-iduronic acid and sulfate content of heparin versus heparan sulfate. |
T3 |
436-690 |
Sentence |
denotes |
Furthermore, the putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-sulfotransferase has been reported to require auxiliary proteins for its N-acetylglucosaminyl N-deacetylase activity in vivo based on its requirement of polycations in vitro. |
T3 |
436-690 |
Sentence |
denotes |
Furthermore, the putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-sulfotransferase has been reported to require auxiliary proteins for its N-acetylglucosaminyl N-deacetylase activity in vivo based on its requirement of polycations in vitro. |
T4 |
691-983 |
Sentence |
denotes |
We have now found that cells derived from embryonic bovine trachea, a tissue that does not synthesize heparin, has a N-acetylglucosaminyl N-deacetylase/N-sulfotransferase, which has 95% amino acid sequence identity to the above enzyme postulated to be involved in the biosynthesis of heparin. |
T4 |
691-983 |
Sentence |
denotes |
We have now found that cells derived from embryonic bovine trachea, a tissue that does not synthesize heparin, has a N-acetylglucosaminyl N-deacetylase/N-sulfotransferase, which has 95% amino acid sequence identity to the above enzyme postulated to be involved in the biosynthesis of heparin. |
T5 |
984-1050 |
Sentence |
denotes |
Both enzymes also have very similar affinity for their substrates. |
T5 |
984-1050 |
Sentence |
denotes |
Both enzymes also have very similar affinity for their substrates. |
T6 |
1051-1322 |
Sentence |
denotes |
The trachea enzyme does not require additional effectors for its N-acetylglucosaminyl N-deacetylase activity in vitro even though its biochemical characteristics are virtually the same as the enzyme previously isolated from cells of a heparin-producing mastocytoma tumor. |
T6 |
1051-1322 |
Sentence |
denotes |
The trachea enzyme does not require additional effectors for its N-acetylglucosaminyl N-deacetylase activity in vitro even though its biochemical characteristics are virtually the same as the enzyme previously isolated from cells of a heparin-producing mastocytoma tumor. |
T7 |
1323-1565 |
Sentence |
denotes |
The trachea enzyme, which is encoded by an abundant 4.6-kilobase mRNA, like mastocytoma cells, has 70% amino acid sequence identity with the corresponding enzyme from rat liver postulated to participate in the biosynthesis of heparan sulfate. |
T7 |
1323-1565 |
Sentence |
denotes |
The trachea enzyme, which is encoded by an abundant 4.6-kilobase mRNA, like mastocytoma cells, has 70% amino acid sequence identity with the corresponding enzyme from rat liver postulated to participate in the biosynthesis of heparan sulfate. |
T8 |
1566-1682 |
Sentence |
denotes |
Heparan sulfate synthesized by trachea cells has a higher content of sulfated iduronic acid than from other tissues. |
T8 |
1566-1682 |
Sentence |
denotes |
Heparan sulfate synthesized by trachea cells has a higher content of sulfated iduronic acid than from other tissues. |
T9 |
1683-2082 |
Sentence |
denotes |
Together, the above results strongly suggest that the above enzymes from mastocytoma, liver, and trachea, per se, are not solely responsible for the selective tissue-specific synthesis of heparin or heparan sulfate; more likely cellular factors, additional enzymes, and availability of substrates in the Golgi lumen also play important roles in the differential synthesis of the above proteoglycans. |
T9 |
1683-2082 |
Sentence |
denotes |
Together, the above results strongly suggest that the above enzymes from mastocytoma, liver, and trachea, per se, are not solely responsible for the selective tissue-specific synthesis of heparin or heparan sulfate; more likely cellular factors, additional enzymes, and availability of substrates in the Golgi lumen also play important roles in the differential synthesis of the above proteoglycans. |