Purification and Properties of Glutathione Reductase of Human Erythrocytes

Meldrum and Tarr (1) reported the presence in red cells of an enzyme that reduces oxidized glutathione (GSSG). Francoeur and Denstedt (2) studied the GSSG-reducing capacity of hemolysates and reported that the reduced forms of both diand triphosphopyridme nucleotide are active in this system. Beutler and Yeh (3) have recently described an 85-fold purification of this enzyme from human red cells. They were unable to separate the DPNH and TPNH activities of the cells by chromatography. The present report describes the properties of a glutathione reductase purified 18,000-fold from human erythrocytes. It is active with both TPNH and DPNH and can also act as a dihydrolipoic dehydrogenase.