Abstract
Two types of reduced pyridine nucleotide dehydrogenase have been characterized in erythrocytes with respect to electron acceptors and donors. Both enzymes have reducing activity towards dyes such as 2,6-dichlorophenolindophenol (DCIP) and methylene blue. Cytochrome b 5 and ferricyanide reductase activity are characteristic to only one of the dehydrogenases. The Reduced pyridine nucleotide specificity of the two enzymes was different. The NADH/NADPH ratio for the former enzyme was 2.9 at pH 7.5; the latter enzyme was specific for NADH only. Methemoglobin prepared by various oxidizing methods was directly reduced by the enzyme plus NADH only. Methylene blue and DCIP effected methemoglobin reduction but the effect of the dyes was different for each enzyme.
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