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Glutathione peroxidase (glutathione:H2O2 oxidoreductase, EC 1.11.1.9) was purified 7500fold from rat erythrocytes and approximately 200 fold from rat liver. The enzyme preparations do not contain impurities which result in interfering reactions. Comparative investigations of enzyme from both liver and erythrocytes do not reveal significant differences in the following points: 1. chromatography on Sephadex G 150; electrophoresis on cellulose acetate strips at pH 5.5—8.0 and varying ionic strength; 3. stability; 4. specificity for the donor substrate; 5. Michaelis constant for H2O2; 6. first order kinetics with regard to GSH. The results confirm the hypothesis that glutathione peroxidase from erythrocytes is identical with the liver enzyme ("contraction factor I"). In view of the established identity it is possible to discuss the biological function of GSH peroxidase in erythrocytes in the light of the numerous results obtained with the liver enzyme. Von NEUBERT, WOJTCZAK und LEHNINGER (1) wurde 1962 ein hitzelabiler Faktor beschrieben, der bei Zugabe von ATP und Mg++ eine Kontraktion von Mitochondrien ermoglichte, die durch Behandlung mit uberphysiologischen Glutathionkonzentrationen eine Schwel

Zur Frage der Identität von Glutathionperoxidase aus Erythrocyten und Leber („Contraction factor I“) der Ratte