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- W2000268460 abstract "At approximately equimolar concentrations (~70 μM), and in the presence of excess catalase and superoxide dismutase, DCIP, ferricytochrome c and ferricyanide abstracted 21, 6 and 61%, respectively, of the electron equivalents given up by NADPH to the NADPH-O2 oxidoreductase complex derived from phorbol myristate acetate-stimulated human neutrophils. With a 10-fold increase in ferricyanide, all of the electron equivalents given up by NADPH to the oxidoreductase complex were shunted to ferricyanide concomitant with complete inhibition of NADPH-dependent O2 consumption. These results substantiate the existence of intrinsic diaphorase activity associated with the superoxide generating NADPH-O2 oxidoreductase of human neutrophils." @default.
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- W2000268460 date "1985-01-01" @default.
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- W2000268460 title "Detection of NADPH diaphorase activity associated with human neutrophil NADPH-O2 oxidoreductase activity" @default.
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- W2000268460 doi "https://doi.org/10.1016/0014-5793(85)80196-4" @default.
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