| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-137 |
Sentence |
denotes |
Human melanoma and Chinese hamster ovary cells galactosylate n-alkyl-beta-glucosides using UDP gal:GlcNAc beta 1,4 galactosyltransferase. |
| T1 |
0-137 |
Sentence |
denotes |
Human melanoma and Chinese hamster ovary cells galactosylate n-alkyl-beta-glucosides using UDP gal:GlcNAc beta 1,4 galactosyltransferase. |
| T1 |
0-137 |
Sentence |
denotes |
Human melanoma and Chinese hamster ovary cells galactosylate n-alkyl-beta-glucosides using UDP gal:GlcNAc beta 1,4 galactosyltransferase. |
| TextSentencer_T2 |
138-270 |
Sentence |
denotes |
We previously showed that human melanoma, CHO and other cells can convert beta-xylosides into structural analogs of ganglioside GM3. |
| T2 |
138-270 |
Sentence |
denotes |
We previously showed that human melanoma, CHO and other cells can convert beta-xylosides into structural analogs of ganglioside GM3. |
| T2 |
138-270 |
Sentence |
denotes |
We previously showed that human melanoma, CHO and other cells can convert beta-xylosides into structural analogs of ganglioside GM3. |
| TextSentencer_T3 |
271-378 |
Sentence |
denotes |
We have investigated several potential acceptors including a series of n-alkyl-beta-D-glucosides (n = 6-9). |
| T3 |
271-378 |
Sentence |
denotes |
We have investigated several potential acceptors including a series of n-alkyl-beta-D-glucosides (n = 6-9). |
| T3 |
271-378 |
Sentence |
denotes |
We have investigated several potential acceptors including a series of n-alkyl-beta-D-glucosides (n = 6-9). |
| TextSentencer_T4 |
379-455 |
Sentence |
denotes |
All were labeled with 3H-galactose when incubated with human melanoma cells. |
| T4 |
379-455 |
Sentence |
denotes |
All were labeled with 3H-galactose when incubated with human melanoma cells. |
| T4 |
379-455 |
Sentence |
denotes |
All were labeled with 3H-galactose when incubated with human melanoma cells. |
| TextSentencer_T5 |
456-612 |
Sentence |
denotes |
Octyl-beta-D-glucoside (Glc beta Octyl) was the best acceptor, whereas neither octyl-alpha-D-glucoside nor N-octanoyl-methylglucamine (MEGA 8) were labeled. |
| T5 |
456-612 |
Sentence |
denotes |
Octyl-beta-D-glucoside (Glc beta Octyl) was the best acceptor, whereas neither octyl-alpha-D-glucoside nor N-octanoyl-methylglucamine (MEGA 8) were labeled. |
| T5 |
456-612 |
Sentence |
denotes |
Octyl-beta-D-glucoside (Glc beta Octyl) was the best acceptor, whereas neither octyl-alpha-D-glucoside nor N-octanoyl-methylglucamine (MEGA 8) were labeled. |
| TextSentencer_T6 |
613-828 |
Sentence |
denotes |
Analysis of the products by a combination of chromatographic methods and specific enzyme digestions showed that the acceptors first received a single Gal beta 1,4 residue followed by an alpha 2,3 linked sialic acid. |
| T6 |
613-828 |
Sentence |
denotes |
Analysis of the products by a combination of chromatographic methods and specific enzyme digestions showed that the acceptors first received a single Gal beta 1,4 residue followed by an alpha 2,3 linked sialic acid. |
| T6 |
613-828 |
Sentence |
denotes |
Analysis of the products by a combination of chromatographic methods and specific enzyme digestions showed that the acceptors first received a single Gal beta 1,4 residue followed by an alpha 2,3 linked sialic acid. |
| TextSentencer_T7 |
829-1012 |
Sentence |
denotes |
Synthesis of these products did not affect cell viability, adherence, protein biosynthesis, or incorporation of radiolabeled precursors into glycoprotein, glycolipid or proteoglycans. |
| T7 |
829-1012 |
Sentence |
denotes |
Synthesis of these products did not affect cell viability, adherence, protein biosynthesis, or incorporation of radiolabeled precursors into glycoprotein, glycolipid or proteoglycans. |
| T7 |
829-1012 |
Sentence |
denotes |
Synthesis of these products did not affect cell viability, adherence, protein biosynthesis, or incorporation of radiolabeled precursors into glycoprotein, glycolipid or proteoglycans. |
| TextSentencer_T8 |
1013-1245 |
Sentence |
denotes |
To determine which beta 1,4 galactosyl transferase synthesized Gal beta 1,4Glc beta Octyl, we analyzed similar incubations using CHO cells and a mutant CHO line (CHO 761) which lacks GAG-core specific beta 1,4 galactosyltransferase. |
| T8 |
1013-1245 |
Sentence |
denotes |
To determine which beta 1,4 galactosyl transferase synthesized Gal beta 1,4Glc beta Octyl, we analyzed similar incubations using CHO cells and a mutant CHO line (CHO 761) which lacks GAG-core specific beta 1,4 galactosyltransferase. |
| T8 |
1013-1245 |
Sentence |
denotes |
To determine which beta 1,4 galactosyl transferase synthesized Gal beta 1,4Glc beta Octyl, we analyzed similar incubations using CHO cells and a mutant CHO line (CHO 761) which lacks GAG-core specific beta 1,4 galactosyltransferase. |
| TextSentencer_T9 |
1246-1357 |
Sentence |
denotes |
The mutant cells showed the same level of incorporation as the control, eliminating this enzyme as a candidate. |
| T9 |
1246-1357 |
Sentence |
denotes |
The mutant cells showed the same level of incorporation as the control, eliminating this enzyme as a candidate. |
| T9 |
1246-1357 |
Sentence |
denotes |
The mutant cells showed the same level of incorporation as the control, eliminating this enzyme as a candidate. |
| TextSentencer_T10 |
1358-1609 |
Sentence |
denotes |
Thermal inactivation kinetics using melanoma cell microsomes and rat liver Golgi to galactosylate Glc beta Octyl showed the same half-life as UDP-Gal:GlcNAc beta 1,4 galactosyltransferase, whereas LacCer synthase was inactivated at a much faster rate. |
| T10 |
1358-1609 |
Sentence |
denotes |
Thermal inactivation kinetics using melanoma cell microsomes and rat liver Golgi to galactosylate Glc beta Octyl showed the same half-life as UDP-Gal:GlcNAc beta 1,4 galactosyltransferase, whereas LacCer synthase was inactivated at a much faster rate. |
| T10 |
1358-1609 |
Sentence |
denotes |
Thermal inactivation kinetics using melanoma cell microsomes and rat liver Golgi to galactosylate Glc beta Octyl showed the same half-life as UDP-Gal:GlcNAc beta 1,4 galactosyltransferase, whereas LacCer synthase was inactivated at a much faster rate. |
| TextSentencer_T11 |
1610-1724 |
Sentence |
denotes |
We show that Glc beta Octyl is a substrate for purified bovine milk UDP-Gal:GlcNAc beta 1,4 galactosyltransferase. |
| T11 |
1610-1724 |
Sentence |
denotes |
We show that Glc beta Octyl is a substrate for purified bovine milk UDP-Gal:GlcNAc beta 1,4 galactosyltransferase. |
| T11 |
1610-1724 |
Sentence |
denotes |
We show that Glc beta Octyl is a substrate for purified bovine milk UDP-Gal:GlcNAc beta 1,4 galactosyltransferase. |
| TextSentencer_T12 |
1725-1858 |
Sentence |
denotes |
Furthermore, the galactosylation of Glc beta Octyl by CHO cell microsomes can be competitively inhibited by GlcNAc or GlcNAc beta MU. |
| T12 |
1725-1858 |
Sentence |
denotes |
Furthermore, the galactosylation of Glc beta Octyl by CHO cell microsomes can be competitively inhibited by GlcNAc or GlcNAc beta MU. |
| T12 |
1725-1858 |
Sentence |
denotes |
Furthermore, the galactosylation of Glc beta Octyl by CHO cell microsomes can be competitively inhibited by GlcNAc or GlcNAc beta MU. |
| TextSentencer_T13 |
1859-2065 |
Sentence |
denotes |
These results indicate that UDP-Gal:GlcNAc beta 1,4 galactosyltransferase is the enzyme used for the synthesis of the alkyl lactosides when cells or rat liver Golgi are incubated with alkyl beta glucosides. |
| T13 |
1859-2065 |
Sentence |
denotes |
These results indicate that UDP-Gal:GlcNAc beta 1,4 galactosyltransferase is the enzyme used for the synthesis of the alkyl lactosides when cells or rat liver Golgi are incubated with alkyl beta glucosides. |
| T13 |
1859-2065 |
Sentence |
denotes |
These results indicate that UDP-Gal:GlcNAc beta 1,4 galactosyltransferase is the enzyme used for the synthesis of the alkyl lactosides when cells or rat liver Golgi are incubated with alkyl beta glucosides. |