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Molecular Pharmacology, Vol 13, 832-839, Copyright © 1977 by the American Society for Pharmacology and Experimental Therapeutics

The Mechanism of Oxidative Hemolysis Produced by Phenylhydrazine

B. GOLDBERG 1 and A. STERN 1

1 Department of Pharmacology, New York University School of Medicine, New York, New York 10016

Superoxide anion was found to be unimportant in phenylhydrazine-induced hemolysis and destruction of oxyhemoglobin. Phenyldiazene, presumably produced via the 2-electron oxidation of phenylhydrazine by oxyhemoglobin, was found to hemolyze red cells rapidly and convert oxyhemoglobin into methemoglobin, hemichromes, and other hemoglobin breakdown products. Phenyldiazene-induced hemolysis requires the presence of molecular oxygen, although superoxide anion, a known product of the reaction of phenyldiazene with oxygen, was demonstrated not to be the active hemolytic agent. The hemolysis produced in the presence of phenyldiazene and oxygen is related to lipid peroxidation in the red cell membrane. Benzenediazonium ion and benzene, oxidation products of phenylhydrazine, were not found to be hemolytic when compared with equimolar quantities of phenyldiazene. It is concluded that the active hemolytic agent produced from phenylhydrazine in red cells is a phenyldiazene-derived free radical produced by the reaction of phenyldiazene with oxygen, and is most probably the phenyl free radical.

Submitted on August 23, 1976
Accepted on April 11, 1977




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