Umei T, Babior B M, Curnutte J T, Smith R M
Department of Molecular and Experimental Medicine, Research Institute of Scripps Clinic, La Jolla, California 92037.
J Biol Chem. 1991 Apr 5;266(10):6019-22.
The respiratory burst oxidase is a multicomponent membrane-bound enzyme that uses NADPH to reduce oxygen to O2-. When oxidase-containing membranes from activated neutrophils are treated with 0.3 M KCl, the NADPH-binding component of the oxidase elutes from the membranes in an active form. Treatment of this eluate with [32P]NADPH dialdehyde labels an approximately 32-kDa protein that is absent from eluates obtained from normal resting membranes or from resting or activated membranes from patients with one form of chronic granulomatous disease. We propose that this approximately 32-kDa protein is the NADPH-binding component of the oxidase.
呼吸爆发氧化酶是一种多组分膜结合酶，它利用NADPH将氧气还原为超氧阴离子（O2-）。当用0.3M KCl处理来自活化中性粒细胞的含氧化酶膜时，氧化酶的NADPH结合组分以活性形式从膜上洗脱下来。用[32P]NADPH二醛处理该洗脱液可标记一种约32kDa的蛋白质，而从正常静息膜或患有某一形式慢性肉芽肿病患者的静息或活化膜获得的洗脱液中不存在这种蛋白质。我们认为这种约32kDa的蛋白质是氧化酶的NADPH结合组分。
