INACTIVATION OF NADPH OXIDASE FROM HUMAN NEUTROPHILS BY AFFINITY LABELING WITH PYRIDOXAL 5'-DIPHOSPHO-5'-ADENOSINE

被引:6
作者
RAVEL, P
LEDERER, F
机构
[1] CNRS URA 1461, Hôpital Necker, 75743 Paris Cedex 15
关键词
D O I
10.1016/0006-291X(91)92074-T
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
When a particulate NADPH oxidase prepared from phorbol ester-activated human neutrophils was treated with pyridoxal 5′-diphospho-5′-adenosine (PLP-AMP), the superoxide anion-producing activity was inhibited according to affinity labeling kinetics. NADPH afforded a protection against inactivation which was competitive with respect to PLP-AMP; 2′,5′-ADP and 2′-phospho-5′ diphosphoadenosine (ATP ribose) appeared to be as potent as NADPH as protecting agents. NADP+ and ATP were less effective, while ADP and GTP-γ-S did not protect significantly. These results suggest that PLP-AMP can be used, in conjunction with tritiated cyanoborohydride, to identify the elusive NADPH-dependent flavoprotein which is part of the electron transfer chain of NADPH oxidase. © 1991.
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页码:1259 / 1265
页数:7
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