| Literature DB >> 4388010 |
Abstract
Spectrophotometric assay methods are described for glutathione synthetase, gamma-glutamylcysteine synthetase and gamma-glutamyl transpeptidase of erythrocytes. The contents of these enzymes in normal human erythrocytes are reported. Erythrocyte glutathione synthetase is inhibited by ADP; this inhibition is competitive with respect to ATP. gamma-Glutamylcysteine synthetase is subject to feedback inhibition by GSH, and is also inhibited by NADH, and to a lesser extent by NAD(+) and NADPH. This enzyme is irreversibly inactivated by cysteamine.Entities:
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Year: 1969 PMID: 4388010 PMCID: PMC1187513 DOI: 10.1042/bj1110309
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857