| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-170 |
Sentence |
denotes |
Identification and characterization of a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminyltransferase from cercariae of the schistosome Trichobilharzia ocellata. |
| T1 |
0-170 |
Sentence |
denotes |
Identification and characterization of a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminyltransferase from cercariae of the schistosome Trichobilharzia ocellata. |
| T1 |
0-170 |
Sentence |
denotes |
Identification and characterization of a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminyltransferase from cercariae of the schistosome Trichobilharzia ocellata. |
| TextSentencer_T2 |
171-267 |
Sentence |
denotes |
Catalysis of a key step in the synthesis of N,N'-diacetyllactosediamino (lacdiNAc)-type glycans. |
| T2 |
171-267 |
Sentence |
denotes |
Catalysis of a key step in the synthesis of N,N'-diacetyllactosediamino (lacdiNAc)-type glycans. |
| T2 |
171-267 |
Sentence |
denotes |
Catalysis of a key step in the synthesis of N,N'-diacetyllactosediamino (lacdiNAc)-type glycans. |
| TextSentencer_T3 |
268-412 |
Sentence |
denotes |
Three different stages of the avian schistosome Trichobilharzia ocellata appeared to contain a novel N-acetylgalactosaminyltransferase activity. |
| T3 |
268-412 |
Sentence |
denotes |
Three different stages of the avian schistosome Trichobilharzia ocellata appeared to contain a novel N-acetylgalactosaminyltransferase activity. |
| T3 |
268-412 |
Sentence |
denotes |
Three different stages of the avian schistosome Trichobilharzia ocellata appeared to contain a novel N-acetylgalactosaminyltransferase activity. |
| TextSentencer_T4 |
413-624 |
Sentence |
denotes |
To investigate its function in the biosynthesis of schistosome glycoconjugates, the enzyme was partially purified from cercariae, a free-living stage of the parasite, by affinity chromatography on UDP-Sepharose. |
| T4 |
413-624 |
Sentence |
denotes |
To investigate its function in the biosynthesis of schistosome glycoconjugates, the enzyme was partially purified from cercariae, a free-living stage of the parasite, by affinity chromatography on UDP-Sepharose. |
| T4 |
413-914 |
Sentence |
denotes |
To investigate its function in the biosynthesis of schistosome glycoconjugates, the enzyme was partially purified from cercariae, a free-living stage of the parasite, by affinity chromatography on UDP-Sepharose. Acceptor specificity studies showed that the enzyme catalyses the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to oligosaccharides, glycopeptides and glycoproteins carrying a terminally beta-linked N-acetylglucosamine (GlcNAc) residue, regardless of the underlying structure. |
| TextSentencer_T5 |
625-914 |
Sentence |
denotes |
Acceptor specificity studies showed that the enzyme catalyses the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to oligosaccharides, glycopeptides and glycoproteins carrying a terminally beta-linked N-acetylglucosamine (GlcNAc) residue, regardless of the underlying structure. |
| T5 |
625-914 |
Sentence |
denotes |
Acceptor specificity studies showed that the enzyme catalyses the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to oligosaccharides, glycopeptides and glycoproteins carrying a terminally beta-linked N-acetylglucosamine (GlcNAc) residue, regardless of the underlying structure. |
| TextSentencer_T6 |
915-1152 |
Sentence |
denotes |
Analysis of the products obtained with GlcNAc and a desialylated and degalactosylated diantennary glycopeptide by 400 MHz 1H-NMR spectroscopy revealed that a GalNAc beta 1-->4GlcNAc (N,N'-diacetyllactosediamine,lacdiNAc) unit was formed. |
| T5 |
915-1152 |
Sentence |
denotes |
Analysis of the products obtained with GlcNAc and a desialylated and degalactosylated diantennary glycopeptide by 400 MHz 1H-NMR spectroscopy revealed that a GalNAc beta 1-->4GlcNAc (N,N'-diacetyllactosediamine,lacdiNAc) unit was formed. |
| T6 |
915-1152 |
Sentence |
denotes |
Analysis of the products obtained with GlcNAc and a desialylated and degalactosylated diantennary glycopeptide by 400 MHz 1H-NMR spectroscopy revealed that a GalNAc beta 1-->4GlcNAc (N,N'-diacetyllactosediamine,lacdiNAc) unit was formed. |
| TextSentencer_T7 |
1153-1282 |
Sentence |
denotes |
The enzyme can therefore be described as a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminytransferase (beta 4-GalNAcT). |
| T6 |
1153-1282 |
Sentence |
denotes |
The enzyme can therefore be described as a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminytransferase (beta 4-GalNAcT). |
| T7 |
1153-1282 |
Sentence |
denotes |
The enzyme can therefore be described as a UDP-GalNAc:GlcNAc beta-R beta 1-->4-N-acetylgalactosaminytransferase (beta 4-GalNAcT). |
| TextSentencer_T8 |
1283-1506 |
Sentence |
denotes |
Using specific acceptors, the enzyme could be distinguished from all other beta 4-GalNAcTs described to date, including the one from pituitary gland that is involved in the specific glycosylation of pituitary glycohormones. |
| T7 |
1283-1506 |
Sentence |
denotes |
Using specific acceptors, the enzyme could be distinguished from all other beta 4-GalNAcTs described to date, including the one from pituitary gland that is involved in the specific glycosylation of pituitary glycohormones. |
| T8 |
1283-1506 |
Sentence |
denotes |
Using specific acceptors, the enzyme could be distinguished from all other beta 4-GalNAcTs described to date, including the one from pituitary gland that is involved in the specific glycosylation of pituitary glycohormones. |
| TextSentencer_T9 |
1507-1804 |
Sentence |
denotes |
By contrast, the enzymatic properties of the schistosome beta 4-GalNAcT (except for the sugar-donor specificity) strongly resemble those of the beta 4-galactosyltransferase of higher animals, an enzyme which is known to control the synthesis of Gal1-->4GlcNAc (lacNAc)-type oligosaccharide chains. |
| T8 |
1507-1804 |
Sentence |
denotes |
By contrast, the enzymatic properties of the schistosome beta 4-GalNAcT (except for the sugar-donor specificity) strongly resemble those of the beta 4-galactosyltransferase of higher animals, an enzyme which is known to control the synthesis of Gal1-->4GlcNAc (lacNAc)-type oligosaccharide chains. |
| T9 |
1507-1804 |
Sentence |
denotes |
By contrast, the enzymatic properties of the schistosome beta 4-GalNAcT (except for the sugar-donor specificity) strongly resemble those of the beta 4-galactosyltransferase of higher animals, an enzyme which is known to control the synthesis of Gal1-->4GlcNAc (lacNAc)-type oligosaccharide chains. |
| TextSentencer_T10 |
1805-1914 |
Sentence |
denotes |
By analogy, the beta 4-GalNAcT is concluded to control the key step in the synthesis of lacdiNAc-type chains. |
| T9 |
1805-1914 |
Sentence |
denotes |
By analogy, the beta 4-GalNAcT is concluded to control the key step in the synthesis of lacdiNAc-type chains. |
| T10 |
1805-1914 |
Sentence |
denotes |
By analogy, the beta 4-GalNAcT is concluded to control the key step in the synthesis of lacdiNAc-type chains. |
| TextSentencer_T11 |
1915-2032 |
Sentence |
denotes |
LacdiNAc-type glycans are also common to the mollusc Lymnaea stagnalis, which is the intermediate host of T.ocellata. |
| T10 |
1915-2032 |
Sentence |
denotes |
LacdiNAc-type glycans are also common to the mollusc Lymnaea stagnalis, which is the intermediate host of T.ocellata. |
| T11 |
1915-2032 |
Sentence |
denotes |
LacdiNAc-type glycans are also common to the mollusc Lymnaea stagnalis, which is the intermediate host of T.ocellata. |
| TextSentencer_T12 |
2033-2259 |
Sentence |
denotes |
It is proposed that the schistosome beta 4-GalNAcT functions in the expression of specific carbohydrate structures that contribute to a molecular mimicry, enabling the schistosome to evade the defence system of the snail host. |
| T11 |
2033-2259 |
Sentence |
denotes |
It is proposed that the schistosome beta 4-GalNAcT functions in the expression of specific carbohydrate structures that contribute to a molecular mimicry, enabling the schistosome to evade the defence system of the snail host. |
| T12 |
2033-2259 |
Sentence |
denotes |
It is proposed that the schistosome beta 4-GalNAcT functions in the expression of specific carbohydrate structures that contribute to a molecular mimicry, enabling the schistosome to evade the defence system of the snail host. |