title: Glutathione-dependent protection against oxidative damage of the human red cell membrane.
abstract: Glutathione (GSH) dependent protection against oxidative damage of human red cell membrane was examined. An artificial system was used in which chloroform/methanol-extracted red cell lipids, in the form of liposomes, were subjected to attack by a peroxidation system consisting of ascorbate-Fe3+. Human erythrocytes contained a nondialyzable factor, completely inactivated by heating in a boiling water bath for 3 min, which showed GSH-dependent inhibition against lipid peroxidation and was devoid of GSH peroxidase activity. On the other hand, GSH-S transferase, highly purified by affinity chromatography, had no inhibitory activity. These findings strongly indicate that the GSH-dependent protection against lipid peroxidation of human red cell membrane is mediated by one or more proteins other than GSH peroxidase and GSH-S transferase.
mesh_terms: D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism* / Q000473:pathology; D005227:Fatty Acids; D005978:Glutathione / Q000097:blood / Q000494:pharmacology*; D005979:Glutathione Peroxidase / Q000494:pharmacology; D005982:Glutathione Transferase / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D008054:Lipid Peroxides / Q000037:antagonists & inhibitors* / Q000097:blood / Q000494:pharmacology; D008315:Malondialdehyde / Q000037:antagonists & inhibitors / Q000097:blood; D010101:Oxygen Consumption / Q000187:drug effects*; D013379:Substrate Specificity
chemical_list: D005227:Fatty Acids; D008054:Lipid Peroxides; C013584:lipid peroxidation inhibitor; D008315:Malondialdehyde; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D005978:Glutathione