| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-114 |
Sentence |
denotes |
Different acceptor specificities of two glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate. |
| T1 |
0-114 |
Sentence |
denotes |
Different acceptor specificities of two glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate. |
| T1 |
0-114 |
Sentence |
denotes |
Different acceptor specificities of two glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate. |
| TextSentencer_T2 |
115-260 |
Sentence |
denotes |
The biosynthesis of HNK-1 carbohydrate is mainly regulated by two glucuronyltransferases (GlcAT-P and GlcAT-S) and a sulfotransferase (HNK-1 ST). |
| T2 |
115-260 |
Sentence |
denotes |
The biosynthesis of HNK-1 carbohydrate is mainly regulated by two glucuronyltransferases (GlcAT-P and GlcAT-S) and a sulfotransferase (HNK-1 ST). |
| T2 |
115-260 |
Sentence |
denotes |
The biosynthesis of HNK-1 carbohydrate is mainly regulated by two glucuronyltransferases (GlcAT-P and GlcAT-S) and a sulfotransferase (HNK-1 ST). |
| TextSentencer_T3 |
261-527 |
Sentence |
denotes |
To determine how the two glucuronyltransferases are involved in the biosynthesis of the HNK-1 carbohydrate, we prepared soluble forms of GlcAT-P and GlcAT-S fused with the IgG-binding domain of protein A and then compared the enzymatic properties of the two enzymes. |
| T3 |
261-527 |
Sentence |
denotes |
To determine how the two glucuronyltransferases are involved in the biosynthesis of the HNK-1 carbohydrate, we prepared soluble forms of GlcAT-P and GlcAT-S fused with the IgG-binding domain of protein A and then compared the enzymatic properties of the two enzymes. |
| T3 |
261-527 |
Sentence |
denotes |
To determine how the two glucuronyltransferases are involved in the biosynthesis of the HNK-1 carbohydrate, we prepared soluble forms of GlcAT-P and GlcAT-S fused with the IgG-binding domain of protein A and then compared the enzymatic properties of the two enzymes. |
| TextSentencer_T4 |
528-700 |
Sentence |
denotes |
Both GlcAT-P and GlcAT-S transferred glucuronic acid (GlcA) not only to a glycoprotein acceptor, asialoorosomucoid (ASOR), but also to a glycolipid acceptor, paragloboside. |
| T4 |
528-700 |
Sentence |
denotes |
Both GlcAT-P and GlcAT-S transferred glucuronic acid (GlcA) not only to a glycoprotein acceptor, asialoorosomucoid (ASOR), but also to a glycolipid acceptor, paragloboside. |
| T4 |
528-700 |
Sentence |
denotes |
Both GlcAT-P and GlcAT-S transferred glucuronic acid (GlcA) not only to a glycoprotein acceptor, asialoorosomucoid (ASOR), but also to a glycolipid acceptor, paragloboside. |
| TextSentencer_T5 |
701-838 |
Sentence |
denotes |
The activity of GlcAT-P toward ASOR was enhanced fivefold in the presence of sphingomyelin, but there were no effects on that of GlcAT-S. |
| T5 |
701-838 |
Sentence |
denotes |
The activity of GlcAT-P toward ASOR was enhanced fivefold in the presence of sphingomyelin, but there were no effects on that of GlcAT-S. |
| T5 |
701-975 |
Sentence |
denotes |
The activity of GlcAT-P toward ASOR was enhanced fivefold in the presence of sphingomyelin, but there were no effects on that of GlcAT-S. The activities of the two enzymes toward paragloboside were only detected in the presence of phospholipids such as phosphatidylinositol. |
| TextSentencer_T6 |
839-975 |
Sentence |
denotes |
The activities of the two enzymes toward paragloboside were only detected in the presence of phospholipids such as phosphatidylinositol. |
| T6 |
839-975 |
Sentence |
denotes |
The activities of the two enzymes toward paragloboside were only detected in the presence of phospholipids such as phosphatidylinositol. |
| TextSentencer_T7 |
976-1089 |
Sentence |
denotes |
Kinetic analysis revealed that the K(m) value of GlcAT-P for ASOR was 10 times lower than that for paragloboside. |
| T6 |
976-1089 |
Sentence |
denotes |
Kinetic analysis revealed that the K(m) value of GlcAT-P for ASOR was 10 times lower than that for paragloboside. |
| T7 |
976-1089 |
Sentence |
denotes |
Kinetic analysis revealed that the K(m) value of GlcAT-P for ASOR was 10 times lower than that for paragloboside. |
| TextSentencer_T8 |
1090-1304 |
Sentence |
denotes |
Furthermore, acceptor specificity analysis involving various oligosaccarides revealed that GlcAT-P specifically recognized N-acetyllactosamine (Galbeta1-4GlcNAc) at the nonreducing terminals of acceptor substrates. |
| T7 |
1090-1304 |
Sentence |
denotes |
Furthermore, acceptor specificity analysis involving various oligosaccarides revealed that GlcAT-P specifically recognized N-acetyllactosamine (Galbeta1-4GlcNAc) at the nonreducing terminals of acceptor substrates. |
| T8 |
1090-1304 |
Sentence |
denotes |
Furthermore, acceptor specificity analysis involving various oligosaccarides revealed that GlcAT-P specifically recognized N-acetyllactosamine (Galbeta1-4GlcNAc) at the nonreducing terminals of acceptor substrates. |
| TextSentencer_T9 |
1305-1504 |
Sentence |
denotes |
In contrast, GlcAT-S recognized not only the terminal Galbeta1-4GlcNAc structure but also the Galbeta1-3GlcNAc structure and showed the highest activity toward triantennary N-linked oligosaccharides. |
| T8 |
1305-1504 |
Sentence |
denotes |
In contrast, GlcAT-S recognized not only the terminal Galbeta1-4GlcNAc structure but also the Galbeta1-3GlcNAc structure and showed the highest activity toward triantennary N-linked oligosaccharides. |
| T9 |
1305-1504 |
Sentence |
denotes |
In contrast, GlcAT-S recognized not only the terminal Galbeta1-4GlcNAc structure but also the Galbeta1-3GlcNAc structure and showed the highest activity toward triantennary N-linked oligosaccharides. |
| TextSentencer_T10 |
1505-1624 |
Sentence |
denotes |
GlcAT-P transferred GlcA to NCAM about twice as much as to ASOR, whereas GlcAT-S did not show any activity toward NCAM. |
| T9 |
1505-1624 |
Sentence |
denotes |
GlcAT-P transferred GlcA to NCAM about twice as much as to ASOR, whereas GlcAT-S did not show any activity toward NCAM. |
| T10 |
1505-1624 |
Sentence |
denotes |
GlcAT-P transferred GlcA to NCAM about twice as much as to ASOR, whereas GlcAT-S did not show any activity toward NCAM. |
| TextSentencer_T11 |
1625-1852 |
Sentence |
denotes |
These lines of evidence indicate that these two enzymes have significantly different acceptor specificities, suggesting that they may synthesize functionally and structurally different HNK-1 carbohydrates in the nervous system. |
| T10 |
1625-1852 |
Sentence |
denotes |
These lines of evidence indicate that these two enzymes have significantly different acceptor specificities, suggesting that they may synthesize functionally and structurally different HNK-1 carbohydrates in the nervous system. |
| T11 |
1625-1852 |
Sentence |
denotes |
These lines of evidence indicate that these two enzymes have significantly different acceptor specificities, suggesting that they may synthesize functionally and structurally different HNK-1 carbohydrates in the nervous system. |