FEBS Letters | |
Detection of NADPH diaphorase activity associated with human neutrophil NADPH‐O2 oxidoreductase activity | |
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
【 预 览 】
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RO201912020286218ZK.pdf | 472KB | download |