Studies in the enzymology of glutathione metabolism in human erythrocytes.
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.
D000217:Acyltransferases / Q000032:analysis; D000227:Adenine Nucleotides / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000378:metabolism; D003543:Cysteamine / Q000494:pharmacology; D003864:Depression, Chemical; D004912:Erythrocytes / Q000201:enzymology*; D005246:Feedback; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D008025:Ligases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D009249:NADP / Q000494:pharmacology; D013053:Spectrophotometry
D000227:Adenine Nucleotides; D009243:NAD; D009249:NADP; D003543:Cysteamine; D000255:Adenosine Triphosphate; D000217:Acyltransferases; D008025:Ligases; D005978:Glutathione