| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-88 |
Sentence |
denotes |
Effect of modification of sialic acid on enzymic hydrolysis of gangliosides GM1 and GM2. |
| T1 |
0-88 |
Sentence |
denotes |
Effect of modification of sialic acid on enzymic hydrolysis of gangliosides GM1 and GM2. |
| T2 |
89-245 |
Sentence |
denotes |
In order to understand the mechanism of action of the activator proteins for the enzymic hydrolysis of GM1 (GM1-activator; Li, S.-C. and Li, Y.-T. (1976) J. |
| T2 |
89-245 |
Sentence |
denotes |
In order to understand the mechanism of action of the activator proteins for the enzymic hydrolysis of GM1 (GM1-activator; Li, S.-C. and Li, Y.-T. (1976) J. |
| T3 |
246-251 |
Sentence |
denotes |
Biol. |
| T3 |
246-251 |
Sentence |
denotes |
Biol. |
| T4 |
252-257 |
Sentence |
denotes |
Chem. |
| T4 |
252-257 |
Sentence |
denotes |
Chem. |
| T5 |
258-333 |
Sentence |
denotes |
251, 1159-1163; for ganglioside designations, see Svennerholm, L. (1963) J. |
| T5 |
258-333 |
Sentence |
denotes |
251, 1159-1163; for ganglioside designations, see Svennerholm, L. (1963) J. |
| T6 |
334-344 |
Sentence |
denotes |
Neurochem. |
| T6 |
334-344 |
Sentence |
denotes |
Neurochem. |
| T7 |
345-429 |
Sentence |
denotes |
10, 613) and GM2 (GM2-activator; Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. |
| T7 |
345-429 |
Sentence |
denotes |
10, 613) and GM2 (GM2-activator; Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. |
| T8 |
430-435 |
Sentence |
denotes |
Biol. |
| T8 |
430-435 |
Sentence |
denotes |
Biol. |
| T9 |
436-441 |
Sentence |
denotes |
Chem. |
| T9 |
436-441 |
Sentence |
denotes |
Chem. |
| T10 |
442-596 |
Sentence |
denotes |
256, 6234-6240), we have studied the effect of chemical modifications of GM1 and GM2 on their susceptibility to the activator-assisted enzymic hydrolysis. |
| T10 |
442-596 |
Sentence |
denotes |
256, 6234-6240), we have studied the effect of chemical modifications of GM1 and GM2 on their susceptibility to the activator-assisted enzymic hydrolysis. |
| T11 |
597-758 |
Sentence |
denotes |
Chemically modified GM1 and GM2 were prepared by methyl esterification (Me-GM1 or Me-GM2) and reduction (HO-GM1 or HO-GM2) of the -COO- group of the sialic acid. |
| T11 |
597-758 |
Sentence |
denotes |
Chemically modified GM1 and GM2 were prepared by methyl esterification (Me-GM1 or Me-GM2) and reduction (HO-GM1 or HO-GM2) of the -COO- group of the sialic acid. |
| T12 |
759-912 |
Sentence |
denotes |
Me-GM1 and HO-GM1 could be hydrolyzed by human hepatic beta-galactosidase in the presence of GM1-activator at rates comparable to that of the native GM1. |
| T12 |
759-912 |
Sentence |
denotes |
Me-GM1 and HO-GM1 could be hydrolyzed by human hepatic beta-galactosidase in the presence of GM1-activator at rates comparable to that of the native GM1. |
| T13 |
913-1072 |
Sentence |
denotes |
However, in contrast to native GM2, Me-GM2 and HO-GM2 were resistant to the hydrolysis by human hepatic beta-hexosaminidase A in the presence of GM2-activator. |
| T13 |
913-1072 |
Sentence |
denotes |
However, in contrast to native GM2, Me-GM2 and HO-GM2 were resistant to the hydrolysis by human hepatic beta-hexosaminidase A in the presence of GM2-activator. |
| T14 |
1073-1216 |
Sentence |
denotes |
When GM2-activator was replaced by sodium taurodeoxycholate, the native GM2 and both modified GM2 could be hydrolyzed by beta-hexosaminidase A. |
| T14 |
1073-1216 |
Sentence |
denotes |
When GM2-activator was replaced by sodium taurodeoxycholate, the native GM2 and both modified GM2 could be hydrolyzed by beta-hexosaminidase A. |
| T15 |
1217-1387 |
Sentence |
denotes |
These results suggest that the carboxyl function of sialic acid in GM1 is not vital for beta-galactosidase or GM1-activator to carry out the cleavage of the terminal Gal. |
| T15 |
1217-1387 |
Sentence |
denotes |
These results suggest that the carboxyl function of sialic acid in GM1 is not vital for beta-galactosidase or GM1-activator to carry out the cleavage of the terminal Gal. |
| T16 |
1388-1506 |
Sentence |
denotes |
In the case of GM2 hydrolysis, the carboxyl function of sialic acid is involved in the interaction with GM2-activator. |
| T16 |
1388-1506 |
Sentence |
denotes |
In the case of GM2 hydrolysis, the carboxyl function of sialic acid is involved in the interaction with GM2-activator. |
| T17 |
1507-1702 |
Sentence |
denotes |
Our results also indicate that the mode of action of GM1-activator is different from that of GM2-activator and that the action of GM2-activator is different from that of sodium taurodeoxycholate. |
| T17 |
1507-1702 |
Sentence |
denotes |
Our results also indicate that the mode of action of GM1-activator is different from that of GM2-activator and that the action of GM2-activator is different from that of sodium taurodeoxycholate. |