Mechanism of the hydrogen peroxide hemolysis test and its reversal with phenols

Abstract

demonstrated that the vitamin E-deficient rat erythrocyte is hemolyzed by a variety of oxidizing agents both in vivo and in vitro. Tsen and Collier (2) and Bunyan Ct al. (3) have shown that hemolysis of the E-deficient rat erythrocyte by dialuric acid is accompanied by lipid peroxidation and that vitamin E and other agents that inhibit hemolysis also inhibit lipid peroxidation. Recently, Jacob and Lux (4) have investigated the response of the E-deficient rat erythrocyte to chronic hydrogen peroxide exposure in vitro. They have demonstrated that loss of phosphatidyl ethanolamine parallels hemolysis and that high molecular weight dextrans inhibit hemolysis. These authors have suggested, therefore, that phosphatidyl ethanolamine is the lipid fraction most susceptible to peroxidation and that peroxidation in this fraction causes sufficient membrane damage to allow colbid osmotic lysis. Horwitt et al. (5) have demonstrated that the E-deficient human erythrocyte is hemolyzed by hydrogen peroxide and that this hemolysis is accompanied by lipid peroxidation. It seemed reasonable, therefore, to suppose that hemolysis of the E-deficient human erythrocyte by hydrogen peroxide was due to lipid peroxidation that would proceed uninhibited in the absence of vitamin E. We have tested this concept using E-deficient infant erythrocytes and have attempted to clarify the nature of the action of H202 in initiating hemolysis and the nature of the action of vitamin E in inhibiting hemolysis.