Detection of NADPH diaphorase activity associated with human neutrophil NADPH‐O2 oxidoreductase activity

FEBS Letters

Green, Terrence R.¹  Wu, David E.¹ 

[1] Department of Clinical Pathology, Veterans Administration Medical Center and Department of Biochemistry, Oregon Health Sciences University, Portland, OR 97201, USA

关键词: NADPH-O2 oxidoreductase;    Superoxide;    NADPH diaphorase neutrophil;    DCIP;    2;    6-dichlorophenolindophenol;    DTPA;    diethylenetriaminepentaacetic acid;    CGD;    chronic granulomatous disease;    PMA;    phorbol myristate acetate;    SOD;    Superoxide dismutase;   

DOI  :  10.1016/0014-5793(85)80196-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown