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Red blood cells (RBCs) from 15 normal human blood samples were incubated with different concentrations of hydrogen peroxide in sodium azide, and the effects of the peroxidation on several glycolytic and nucleotidic enzyme activities were investigated. The release of malonyl dialdehyde (MDA) and methemoglobin formation were used as indicators of RBC peroxidation. The increase of H(2)O(2), final concentration from 0.1 to 5 mmol/1, resulted in a progressive rise of almost all glycolytic enzyme activities, especially those of aldolase (200% of normal at 1 mmol/1), phosphoglycerate kinase (140%), phosphoglycerate mutase (136%), pyruvate kinase (130%) and glutathione peroxidase (130%), and in a decrease of glucose-6-phosphate dehydrogenase (68%) and pyrimidine-5-nucleotidase (23%). The addition of ß-mercaptoethanol to the incubation medium abolished only the effect of 1 mmol/1 H(2)O(2) on glucose-6-phosphate dehydrogenase.

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