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Title: Inactivation of NADPH oxidase from human neutrophils by affinity labeling with pyridoxal 5'-diphospho-5'-adenosine. Author: Ravel P, Lederer F. Journal: Biochem Biophys Res Commun; 1991 Dec 31; 181(3):1259-65. PubMed ID: 1764075. Abstract: 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-gamma-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.[Abstract] [Full Text] [Related] [New Search]