Abstract
The activity of glutathione peroxidase (H2O2:glutathione oxidoreductase, EC 1.11.1.9) has been studied in the soluble supernatant fractions prepared from rat liver homogenates. Enzyme activity may be demonstrated in the presence of active as well as inhibited catalase. The findings are compatible with an essential function for hepatic glutathione peroxidase in the detoxication of intracellular hydrogen peroxide, and with the view that hydrogen peroxide is the common toxic agent in the drug-induced anemia associated with a genetic deficiency of erythrocyte glucose 6-phosphate dehydrogenase. The experiments also suggest a potential role for glutathione peroxidase in regulating cellular metabolism via pentose shunt control.
- Copyright ©, 1968, by Academic Press Inc.
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