Studies in the enzymology of glutathione metabolism in human erythrocytes

Author:

Jackson R. C.1

Affiliation:

1. Chester Beatty Research Institute, Institute of Cancer Research: Royal Cancer Hospital, London, S.W. 3

Abstract

Spectrophotometric assay methods are described for glutathione synthetase, γ-glutamylcysteine synthetase and γ-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. γ-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.

Publisher

Portland Press Ltd.

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2. Glutathione Synthesis and Turnover in the Human Erythrocyte;Journal of Biological Chemistry;2010-07

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