The function of subcellular fractions in the oxidation of glutathione in rat liver homogenate.
1. The aerobic loss of GSH added to the supernatant fraction from rat liver is much increased by including the microsome fraction, which both inhibits the concurrent reduction of the GSSG formed and also augments the net oxidation rate. 2. Oxidation occurs with a mixture of dialysed supernatant and a protein-free filtrate; the latter is replaceable by hypoxanthine and the former by xanthine oxidase, whereas fractions lacking this enzyme give no oxidation. 3. In all these instances augmentation occurs with microsomes, with fractions having urate oxidase activity and with the purified enzyme; uric acid and microsomes alone also support the oxidation. 4. Evidence implicating additional protein factors is discussed. 5. It is suggested that GSH oxidation by homogenate is linked through glutathione peroxidase to the reaction of endogenous substrate with supernatant xanthine oxidase and of the uric acid formed with peroxisomal urate oxidase.
D000818:Animals; D003956:Dialysis; D005978:Glutathione / Q000378:metabolism*; D007042:Hypoxanthines / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D051381:Rats; D014020:Tissue Extracts; D014503:Urate Oxidase / Q000378:metabolism; D014527:Uric Acid / Q000378:metabolism; D014969:Xanthine Oxidase / Q000378:metabolism
D007042:Hypoxanthines; D011506:Proteins; D014020:Tissue Extracts; D014527:Uric Acid; D010544:Peroxidases; D014969:Xanthine Oxidase; D014503:Urate Oxidase; D005978:Glutathione