Detection of NADPH diaphorase activity associated with human neutrophil NADPH‐O2 oxidoreductase activity
- 1 January 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 179 (1) , 82-86
- https://doi.org/10.1016/0014-5793(85)80196-4
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.Keywords
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