| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-137 |
Sentence |
denotes |
Comparison of the substrate specificities and catalytic properties of the sister N-acetylglucosaminyltransferases, GnT-V and GnT-Vb (IX). |
| T1 |
0-137 |
Sentence |
denotes |
Comparison of the substrate specificities and catalytic properties of the sister N-acetylglucosaminyltransferases, GnT-V and GnT-Vb (IX). |
| T1 |
0-137 |
Sentence |
denotes |
Comparison of the substrate specificities and catalytic properties of the sister N-acetylglucosaminyltransferases, GnT-V and GnT-Vb (IX). |
| TextSentencer_T2 |
138-255 |
Sentence |
denotes |
N-Acetylglucosaminlyltransferase-V (GnT-V) synthesizes GlcNAcbeta1,6Man branched N-glycans both in vitro and in vivo. |
| T2 |
138-255 |
Sentence |
denotes |
N-Acetylglucosaminlyltransferase-V (GnT-V) synthesizes GlcNAcbeta1,6Man branched N-glycans both in vitro and in vivo. |
| T2 |
138-255 |
Sentence |
denotes |
N-Acetylglucosaminlyltransferase-V (GnT-V) synthesizes GlcNAcbeta1,6Man branched N-glycans both in vitro and in vivo. |
| TextSentencer_T3 |
256-369 |
Sentence |
denotes |
A paralog, GnT-Vb (or GnT-IX), has also been shown to synthesize both GlcNAcbeta1,6Man branched N- and O-glycans. |
| T3 |
256-369 |
Sentence |
denotes |
A paralog, GnT-Vb (or GnT-IX), has also been shown to synthesize both GlcNAcbeta1,6Man branched N- and O-glycans. |
| T3 |
256-369 |
Sentence |
denotes |
A paralog, GnT-Vb (or GnT-IX), has also been shown to synthesize both GlcNAcbeta1,6Man branched N- and O-glycans. |
| TextSentencer_T4 |
370-492 |
Sentence |
denotes |
GnT-V is expressed in most human and rodent tissues while GnT-Vb expression is limited mainly to neural tissue and testes. |
| T4 |
370-492 |
Sentence |
denotes |
GnT-V is expressed in most human and rodent tissues while GnT-Vb expression is limited mainly to neural tissue and testes. |
| T4 |
370-492 |
Sentence |
denotes |
GnT-V is expressed in most human and rodent tissues while GnT-Vb expression is limited mainly to neural tissue and testes. |
| TextSentencer_T5 |
493-605 |
Sentence |
denotes |
It is of interest, therefore, to compare the catalytic properties and reaction kinetics of these sister enzymes. |
| T5 |
493-605 |
Sentence |
denotes |
It is of interest, therefore, to compare the catalytic properties and reaction kinetics of these sister enzymes. |
| T5 |
493-605 |
Sentence |
denotes |
It is of interest, therefore, to compare the catalytic properties and reaction kinetics of these sister enzymes. |
| TextSentencer_T6 |
606-800 |
Sentence |
denotes |
The results demonstrate that while GnT-V was fully active without exogenous cation and in the presence of EDTA, the activity of GnT-Vb was stimulated over 4-fold in the presence of 10 mM Mn(++). |
| T6 |
606-800 |
Sentence |
denotes |
The results demonstrate that while GnT-V was fully active without exogenous cation and in the presence of EDTA, the activity of GnT-Vb was stimulated over 4-fold in the presence of 10 mM Mn(++). |
| T6 |
606-800 |
Sentence |
denotes |
The results demonstrate that while GnT-V was fully active without exogenous cation and in the presence of EDTA, the activity of GnT-Vb was stimulated over 4-fold in the presence of 10 mM Mn(++). |
| TextSentencer_T7 |
801-933 |
Sentence |
denotes |
The pH optimum for GnT-V was in the range of 6.5-7.0, while that of GnT-Vb was 8.0. common for glycosyltransferases active in brain. |
| T7 |
801-933 |
Sentence |
denotes |
The pH optimum for GnT-V was in the range of 6.5-7.0, while that of GnT-Vb was 8.0. common for glycosyltransferases active in brain. |
| T7 |
801-933 |
Sentence |
denotes |
The pH optimum for GnT-V was in the range of 6.5-7.0, while that of GnT-Vb was 8.0. common for glycosyltransferases active in brain. |
| TextSentencer_T8 |
934-1154 |
Sentence |
denotes |
Both enzymes transferred GlcNAcbeta1,6 to the Man residue of the GlcNAcbeta1,2Man moiety of glycan substrates, and both enzymes acted effectively on a synthetic GlcNAcbeta1,2Manalpha1,2Glc-O-octyl trisaccharide acceptor. |
| T8 |
934-1154 |
Sentence |
denotes |
Both enzymes transferred GlcNAcbeta1,6 to the Man residue of the GlcNAcbeta1,2Man moiety of glycan substrates, and both enzymes acted effectively on a synthetic GlcNAcbeta1,2Manalpha1,2Glc-O-octyl trisaccharide acceptor. |
| T8 |
934-1154 |
Sentence |
denotes |
Both enzymes transferred GlcNAcbeta1,6 to the Man residue of the GlcNAcbeta1,2Man moiety of glycan substrates, and both enzymes acted effectively on a synthetic GlcNAcbeta1,2Manalpha1,2Glc-O-octyl trisaccharide acceptor. |
| TextSentencer_T9 |
1155-1340 |
Sentence |
denotes |
Moreover, although both enzymes utilized an N-linked asialo-agalacto-biantennary glycan as an acceptor, GnT-Vb displayed an almost 2.5-fold higher apparent K(m) value compared to GnT-V. |
| T9 |
1155-1340 |
Sentence |
denotes |
Moreover, although both enzymes utilized an N-linked asialo-agalacto-biantennary glycan as an acceptor, GnT-Vb displayed an almost 2.5-fold higher apparent K(m) value compared to GnT-V. |
| T9 |
1155-1800 |
Sentence |
denotes |
Moreover, although both enzymes utilized an N-linked asialo-agalacto-biantennary glycan as an acceptor, GnT-Vb displayed an almost 2.5-fold higher apparent K(m) value compared to GnT-V. Conversely, GnT-Vb very efficiently glycosylated a synthetic glycopeptide, Ac-H(2)N-Val-Glu-Pro-(GlcNAcbeta1,2-Man-O-)Thr-Ala-Val-CO-Ac, while GnT-V showed relatively poor activity toward this O-Man-linked glycopeptide acceptor, with a K(m) value of 20-fold higher than that of GnT-Vb. When the N-linked asialo-agalacto-biantennary glycan acceptor was utilized with GnT-Vb, the expected triantennary beta1,6-branched product was observed up to 8 h incubation. |
| TextSentencer_T10 |
1341-1626 |
Sentence |
denotes |
Conversely, GnT-Vb very efficiently glycosylated a synthetic glycopeptide, Ac-H(2)N-Val-Glu-Pro-(GlcNAcbeta1,2-Man-O-)Thr-Ala-Val-CO-Ac, while GnT-V showed relatively poor activity toward this O-Man-linked glycopeptide acceptor, with a K(m) value of 20-fold higher than that of GnT-Vb. |
| T10 |
1341-1626 |
Sentence |
denotes |
Conversely, GnT-Vb very efficiently glycosylated a synthetic glycopeptide, Ac-H(2)N-Val-Glu-Pro-(GlcNAcbeta1,2-Man-O-)Thr-Ala-Val-CO-Ac, while GnT-V showed relatively poor activity toward this O-Man-linked glycopeptide acceptor, with a K(m) value of 20-fold higher than that of GnT-Vb. |
| TextSentencer_T11 |
1627-1800 |
Sentence |
denotes |
When the N-linked asialo-agalacto-biantennary glycan acceptor was utilized with GnT-Vb, the expected triantennary beta1,6-branched product was observed up to 8 h incubation. |
| T11 |
1627-1800 |
Sentence |
denotes |
When the N-linked asialo-agalacto-biantennary glycan acceptor was utilized with GnT-Vb, the expected triantennary beta1,6-branched product was observed up to 8 h incubation. |
| TextSentencer_T12 |
1801-1954 |
Sentence |
denotes |
An additional product with two beta1,6-linked GlcNAc resides, however, was observed after prolonged (>8 h) incubation, consistent with an earlier report. |
| T10 |
1801-1954 |
Sentence |
denotes |
An additional product with two beta1,6-linked GlcNAc resides, however, was observed after prolonged (>8 h) incubation, consistent with an earlier report. |
| T12 |
1801-1954 |
Sentence |
denotes |
An additional product with two beta1,6-linked GlcNAc resides, however, was observed after prolonged (>8 h) incubation, consistent with an earlier report. |
| TextSentencer_T13 |
1955-2132 |
Sentence |
denotes |
This unusual tetraantennary product was observed with GnT-Vb only after substantial accumulation of the first triantennary product and not during the early stages of incubation. |
| T11 |
1955-2132 |
Sentence |
denotes |
This unusual tetraantennary product was observed with GnT-Vb only after substantial accumulation of the first triantennary product and not during the early stages of incubation. |
| T13 |
1955-2132 |
Sentence |
denotes |
This unusual tetraantennary product was observed with GnT-Vb only after substantial accumulation of the first triantennary product and not during the early stages of incubation. |