| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-98 |
Sentence |
denotes |
Specific recognition of N-acetylneuraminic acid in the GM2 epitope by human GM2 activator protein. |
| T1 |
0-98 |
Sentence |
denotes |
Specific recognition of N-acetylneuraminic acid in the GM2 epitope by human GM2 activator protein. |
| T2 |
99-399 |
Sentence |
denotes |
GM2 Activator is a low molecular weight protein cofactor that stimulates the enzymatic conversion of GM2 into GM3 by human beta-hexosaminidase A and also the conversion of GM2 into GA2 by clostridial sialidase (Wu, Y.-Y., Lockyer, J.M., Sugiyama, E., Pavlova, N.V., Li, Y.-T., and Li, S.-C. (1994) J. |
| T2 |
99-399 |
Sentence |
denotes |
GM2 Activator is a low molecular weight protein cofactor that stimulates the enzymatic conversion of GM2 into GM3 by human beta-hexosaminidase A and also the conversion of GM2 into GA2 by clostridial sialidase (Wu, Y.-Y., Lockyer, J.M., Sugiyama, E., Pavlova, N.V., Li, Y.-T., and Li, S.-C. (1994) J. |
| T3 |
400-405 |
Sentence |
denotes |
Biol. |
| T3 |
400-405 |
Sentence |
denotes |
Biol. |
| T4 |
406-411 |
Sentence |
denotes |
Chem. |
| T4 |
406-411 |
Sentence |
denotes |
Chem. |
| T5 |
412-430 |
Sentence |
denotes |
269, 16276-16283). |
| T5 |
412-430 |
Sentence |
denotes |
269, 16276-16283). |
| T6 |
431-592 |
Sentence |
denotes |
Among the five known activator proteins for the enzymatic hydrolysis of glycosphingolipids, only GM2 activator is effective in stimulating the hydrolysis of GM2. |
| T6 |
431-592 |
Sentence |
denotes |
Among the five known activator proteins for the enzymatic hydrolysis of glycosphingolipids, only GM2 activator is effective in stimulating the hydrolysis of GM2. |
| T7 |
593-672 |
Sentence |
denotes |
However, the mechanism of action of GM2 activator is still not well understood. |
| T7 |
593-672 |
Sentence |
denotes |
However, the mechanism of action of GM2 activator is still not well understood. |
| T8 |
673-1017 |
Sentence |
denotes |
Using a unique disialosylganglioside, GalNAc-GD1a, as the substrate, we were able to show that in the presence of GM2 activator, GalNAc-GD1a was specifically converted into GalNAc-GM1a by clostridial sialidase, while in the presence of saposin B, a nonspecific activator protein, GalNAc-GD1a was converted into both GalNAc-GM1a and GalNAc-GM1b. |
| T8 |
673-1017 |
Sentence |
denotes |
Using a unique disialosylganglioside, GalNAc-GD1a, as the substrate, we were able to show that in the presence of GM2 activator, GalNAc-GD1a was specifically converted into GalNAc-GM1a by clostridial sialidase, while in the presence of saposin B, a nonspecific activator protein, GalNAc-GD1a was converted into both GalNAc-GM1a and GalNAc-GM1b. |
| T9 |
1018-1251 |
Sentence |
denotes |
Individual products generated from GalNAc-GD1a by clostridial sialidase were identified by thin layer chromatography, negative secondary ion mass spectrometry, and immunostaining with a monoclonal IgM that recognizes the GM2 epitope. |
| T9 |
1018-1251 |
Sentence |
denotes |
Individual products generated from GalNAc-GD1a by clostridial sialidase were identified by thin layer chromatography, negative secondary ion mass spectrometry, and immunostaining with a monoclonal IgM that recognizes the GM2 epitope. |
| T10 |
1252-1338 |
Sentence |
denotes |
Our results clearly show that GM2 activator recognizes the GM2 epitope in GalNAc-GD1a. |
| T10 |
1252-1338 |
Sentence |
denotes |
Our results clearly show that GM2 activator recognizes the GM2 epitope in GalNAc-GD1a. |
| T11 |
1339-1529 |
Sentence |
denotes |
Thus, GM2 activator may interact with the trisaccharide structure of the GM2 epitope and render the GalNAc and NeuAc residues accessible to beta-hexosaminidase A and sialidase, respectively. |
| T11 |
1339-1529 |
Sentence |
denotes |
Thus, GM2 activator may interact with the trisaccharide structure of the GM2 epitope and render the GalNAc and NeuAc residues accessible to beta-hexosaminidase A and sialidase, respectively. |