Erythrocyte Glutathione Reductase

Abstract

Abstract 1. The physiologic roles of glutathione in the red cell and of glutathione reductase are reviewed briefly. 2. The partial purification of glutathione reductase by a combination of salting out, heating and chromatographic procedures is described. 3. Throughout purification, no appreciable change in the ratio of activity of the enzyme with DPN and TPN as a coenzyme has been found. 4. Potassium chloride and sodium chloride increased markedly the enzymatic activity when TPNH served as hydrogen donor. However, when DPNH was the hydrogen donor these salts caused a decrease in enzyme activity. Potassium phosphate buffer increased enzymatic activity with TPNH but produced little change with DPNH. 5. Michaelis-Menten constants were computed for the purified enzyme preparations. 6. The DPN-linked system did not result in GSSG reduction when lactate served as a substrate in intact erythrocytes.