| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-143 |
Sentence |
denotes |
Identification and characterization of a novel UDP-GalNAc:GlcAbeta-R alpha1,4-N-acetylgalactosaminyltransferase from a human sarcoma cell line. |
| T1 |
0-143 |
Sentence |
denotes |
Identification and characterization of a novel UDP-GalNAc:GlcAbeta-R alpha1,4-N-acetylgalactosaminyltransferase from a human sarcoma cell line. |
| T1 |
0-143 |
Sentence |
denotes |
Identification and characterization of a novel UDP-GalNAc:GlcAbeta-R alpha1,4-N-acetylgalactosaminyltransferase from a human sarcoma cell line. |
| TextSentencer_T2 |
144-257 |
Sentence |
denotes |
We recently discovered a novel alpha-N-acetylgalactosaminyltransferase in fetal bovine serum (Kitagawa et al., J. |
| T2 |
144-257 |
Sentence |
denotes |
We recently discovered a novel alpha-N-acetylgalactosaminyltransferase in fetal bovine serum (Kitagawa et al., J. |
| T2 |
144-556 |
Sentence |
denotes |
We recently discovered a novel alpha-N-acetylgalactosaminyltransferase in fetal bovine serum (Kitagawa et al., J. Biol. Chem., 270, 22190-22195, 1995) and also in mouse mast cytoma cells (Lidholt et al., Glycoconjugate J., 14, 737-742, 1997), which catalyzed the transfer of an alpha-GalNAc residue to the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, derived from proteoglycans. |
| TextSentencer_T3 |
258-263 |
Sentence |
denotes |
Biol. |
| T3 |
258-263 |
Sentence |
denotes |
Biol. |
| TextSentencer_T4 |
264-556 |
Sentence |
denotes |
Chem., 270, 22190-22195, 1995) and also in mouse mast cytoma cells (Lidholt et al., Glycoconjugate J., 14, 737-742, 1997), which catalyzed the transfer of an alpha-GalNAc residue to the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, derived from proteoglycans. |
| T4 |
264-556 |
Sentence |
denotes |
Chem., 270, 22190-22195, 1995) and also in mouse mast cytoma cells (Lidholt et al., Glycoconjugate J., 14, 737-742, 1997), which catalyzed the transfer of an alpha-GalNAc residue to the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, derived from proteoglycans. |
| TextSentencer_T5 |
557-762 |
Sentence |
denotes |
In this study, we characterized this enzyme using a preparation obtained from the serum-free culture medium of a human sarcoma (malignant fibrous histiocytoma) cell line by phenyl-Sepharose chromatography. |
| T3 |
557-762 |
Sentence |
denotes |
In this study, we characterized this enzyme using a preparation obtained from the serum-free culture medium of a human sarcoma (malignant fibrous histiocytoma) cell line by phenyl-Sepharose chromatography. |
| T5 |
557-762 |
Sentence |
denotes |
In this study, we characterized this enzyme using a preparation obtained from the serum-free culture medium of a human sarcoma (malignant fibrous histiocytoma) cell line by phenyl-Sepharose chromatography. |
| TextSentencer_T6 |
763-1043 |
Sentence |
denotes |
Structural characterization by1H NMR spectroscopy of the reaction product using the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, as a substrate demonstrated that the enzyme was a UDP-GalNAc:GlcAbeta1-R alpha1,4-N -acetylgalactosaminyltransferase. |
| T4 |
763-1043 |
Sentence |
denotes |
Structural characterization by1H NMR spectroscopy of the reaction product using the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, as a substrate demonstrated that the enzyme was a UDP-GalNAc:GlcAbeta1-R alpha1,4-N -acetylgalactosaminyltransferase. |
| T6 |
763-1043 |
Sentence |
denotes |
Structural characterization by1H NMR spectroscopy of the reaction product using the linkage tetrasaccharide-serine, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, as a substrate demonstrated that the enzyme was a UDP-GalNAc:GlcAbeta1-R alpha1,4-N -acetylgalactosaminyltransferase. |
| TextSentencer_T7 |
1044-1126 |
Sentence |
denotes |
This is the first identification of an alpha1,4-N-acetylgalactosaminyltransferase. |
| T5 |
1044-1126 |
Sentence |
denotes |
This is the first identification of an alpha1,4-N-acetylgalactosaminyltransferase. |
| T7 |
1044-1126 |
Sentence |
denotes |
This is the first identification of an alpha1,4-N-acetylgalactosaminyltransferase. |
| TextSentencer_T8 |
1127-1478 |
Sentence |
denotes |
Using N -acetylchondrosine GlcAbeta1-3GalNAc as an alternative substrate, the enzyme required divalent cations for the transferase reaction, with maximal activity at 20 mM Mn2+and exhibited a dual optimum at pH 6.5 and pH 7.4 depending upon the buffers used, with the highest activity in a 50 mM 2-( N -morpholino)ethanesulfonic acid buffer at pH 6.5. |
| T6 |
1127-1478 |
Sentence |
denotes |
Using N -acetylchondrosine GlcAbeta1-3GalNAc as an alternative substrate, the enzyme required divalent cations for the transferase reaction, with maximal activity at 20 mM Mn2+and exhibited a dual optimum at pH 6.5 and pH 7.4 depending upon the buffers used, with the highest activity in a 50 mM 2-( N -morpholino)ethanesulfonic acid buffer at pH 6.5. |
| T8 |
1127-1478 |
Sentence |
denotes |
Using N -acetylchondrosine GlcAbeta1-3GalNAc as an alternative substrate, the enzyme required divalent cations for the transferase reaction, with maximal activity at 20 mM Mn2+and exhibited a dual optimum at pH 6.5 and pH 7.4 depending upon the buffers used, with the highest activity in a 50 mM 2-( N -morpholino)ethanesulfonic acid buffer at pH 6.5. |
| TextSentencer_T9 |
1479-1646 |
Sentence |
denotes |
The apparent Km values obtained for N -acetylchondrosine, the linkage tetrasaccharide-serine, and UDP-GalNAc were 1060 microM, 188 microM, and 27 microM, respectively. |
| T7 |
1479-1646 |
Sentence |
denotes |
The apparent Km values obtained for N -acetylchondrosine, the linkage tetrasaccharide-serine, and UDP-GalNAc were 1060 microM, 188 microM, and 27 microM, respectively. |
| T9 |
1479-1646 |
Sentence |
denotes |
The apparent Km values obtained for N -acetylchondrosine, the linkage tetrasaccharide-serine, and UDP-GalNAc were 1060 microM, 188 microM, and 27 microM, respectively. |
| TextSentencer_T10 |
1647-1747 |
Sentence |
denotes |
This suggested that the linkage tetrasaccharide-serine was a good acceptor substrate for the enzyme. |
| T8 |
1647-1747 |
Sentence |
denotes |
This suggested that the linkage tetrasaccharide-serine was a good acceptor substrate for the enzyme. |
| T10 |
1647-1747 |
Sentence |
denotes |
This suggested that the linkage tetrasaccharide-serine was a good acceptor substrate for the enzyme. |
| TextSentencer_T11 |
1748-2021 |
Sentence |
denotes |
In addition, the enzyme utilized glucuronylneolactotetraosylceramide GlcAbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4G lcbeta1-1Cer but not sulfoglucuronylneolactotetraosylceramide GlcA(3-O -sulfate)beta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cbeta1-1Cer as acceptor substrates. |
| T9 |
1748-2021 |
Sentence |
denotes |
In addition, the enzyme utilized glucuronylneolactotetraosylceramide GlcAbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4G lcbeta1-1Cer but not sulfoglucuronylneolactotetraosylceramide GlcA(3-O -sulfate)beta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cbeta1-1Cer as acceptor substrates. |
| T11 |
1748-2021 |
Sentence |
denotes |
In addition, the enzyme utilized glucuronylneolactotetraosylceramide GlcAbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4G lcbeta1-1Cer but not sulfoglucuronylneolactotetraosylceramide GlcA(3-O -sulfate)beta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cbeta1-1Cer as acceptor substrates. |
| TextSentencer_T12 |
2022-2171 |
Sentence |
denotes |
The possibility of involvement of this enzyme in the biosynthesis of glycosaminoglycan as well as other GlcA-containing glycoconjugates is discussed. |
| T10 |
2022-2171 |
Sentence |
denotes |
The possibility of involvement of this enzyme in the biosynthesis of glycosaminoglycan as well as other GlcA-containing glycoconjugates is discussed. |
| T12 |
2022-2171 |
Sentence |
denotes |
The possibility of involvement of this enzyme in the biosynthesis of glycosaminoglycan as well as other GlcA-containing glycoconjugates is discussed. |