Cysteine sulfinate transamination activity of aspartate aminotransferases. |
| |
Authors: | T Yagi H Kagamiyama M Nozaki |
| |
Affiliation: | Department of Biochemistry, Shiga University of Medical Science, Seta, Ohtsu, Shiga, 520-21, Japan |
| |
Abstract: | Aspartate aminotransferases from pig heart cytosol and mitochondria, B and accepted L-cysteine sulfinate as a good substrate. The mitochondrial isoenzyme and the enzyme showed higher activity toward L-cysteine sulfinate than toward the natural substrates, L-glutamate and L-aspartate. The cytosolic isoenzyme catalyzed the L-cysteine sulfinate transamination at 50% the rate of L-glutamate transamination. The enzyme had the same reactivity toward the three substrates. Antisera against the two isoenzymes and the enzyme inactivated almost completely cysteine sulfinate transamination activity in the crude extracts of pig heart muscle and B, respectively. These results indicate that cysteine sulfinate transamination is catalyzed by aspartate aminotransferase in these cells. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|