Sakane F, Kojima H, Takahashi K, Koyama J
Biochem Biophys Res Commun. 1987 Aug 31;147(1):71-7. doi: 10.1016/s0006-291x(87)80088-8.
NADPH-cytochrome c reductase and cytochrome b559 were purified from the membrane fraction of phorbol myristate acetate-stimulated porcine polymorphonuclear leukocytes. The highly purified reductase oxidized NADPH and generated superoxide when combined with partially purified cytochrome b559 in the presence of phosphatidylcholine. In the same system, but under the anaerobic condition, the reductase was found to reduce cytochrome b559.
从佛波醇肉豆蔻酸酯乙酸酯刺激的猪多形核白细胞的膜部分中纯化出NADPH-细胞色素c还原酶和细胞色素b559。在磷脂酰胆碱存在的情况下，高度纯化的还原酶与部分纯化的细胞色素b559结合时会氧化NADPH并产生超氧化物。在相同体系中，但在厌氧条件下，发现该还原酶会还原细胞色素b559。
