黑根霉中孕酮诱导的NADPH-细胞色素c（P-450）还原酶的分解与重组
Resolution and reconstitution of the NADPH-cytochrome c (P-450) reductase induced by progesterone in Rhizopus nigricans.
作者信息
Cresnar B, Breskvar K, Hudnik-Plevnik T
出版信息
Biochem Biophys Res Commun. 1985 Dec 31;133(3):1057-63. doi: 10.1016/0006-291x(85)91243-4.
The NADPH-cytochrome c (P-450) reductase induced in the filamentous fungus Rhizopus nigricans as a component of 11 alpha-hydroxylase of progesterone was resolved by DEAE-cellulose chromatography into two components. One of the components is an iron-sulfur protein (rhizoporedoxin), whereas the other component is a protein with reductase activity dependent on NADPH (rhizoporedoxin reductase). As shown in the reconstitution assay, the NADPH-cytochrome c (P-450) reductase activity was restored upon combination of these two proteins.
在丝状真菌黑根霉中作为孕酮11α-羟化酶的一个组分被诱导产生的NADPH-细胞色素c（P-450）还原酶，通过DEAE-纤维素层析被分离为两个组分。其中一个组分是铁硫蛋白（根霉铁氧还蛋白），而另一个组分是一种具有依赖于NADPH的还原酶活性的蛋白质（根霉铁氧还蛋白还原酶）。如在重组试验中所示，当这两种蛋白质结合时，NADPH-细胞色素c（P-450）还原酶活性得以恢复。
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