| Literature DB >> 6108786 |
P G Board, J E Smith, K Moore, D Ou.
Abstract
gamma-Glutamylcysteine synthetase (L-glutamate:L-cysteine gamma-ligase (ADP-forming), EC 6.3.2.2) was purified from the erythrocytes of normal and low-glutathione sheep. The molecular weight (78 000), pH optimum (pH 7), substrate specificity, inhibition constant for glutathione (0.44-0.50 mM), electrophoretic mobility, and heat stability were similar for the purified enzyme from both sources. Using immunological techniques, the specific activity of gamma-glutamylcysteine synthetase from low-glutathione sheep was lower than that from normal sheep.Entities:
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Year: 1980 PMID: 6108786 DOI: 10.1016/0005-2744(80)90109-6
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002