Boström H
J Lipid Res. 1986 Aug;27(8):807-12.
The properties of the species-specific 6 alpha-hydroxylation of taurochenodeoxycholic acid were studied in subcellular fractions from pig liver. The hydroxylation was observed in microsomes but not in mitochondria. A partially purified cytochrome P-450 fraction in the presence of NADPH-cytochrome P-450 reductase, NADPH, and phospholipid catalyzed 6 alpha-hydroxylation of taurochenodeoxycholic acid at a 160-fold higher rate than the microsomes. This cytochrome P-450 fraction did not catalyze 6 alpha-hydroxylation of 5 beta-cholestane-3 alpha,7 alpha-diol or testosterone, nor did it catalyze 7 alpha-hydroxylation of cholesterol.
在猪肝的亚细胞组分中研究了牛磺鹅去氧胆酸物种特异性6α-羟基化的特性。羟基化在微粒体中观察到,但在线粒体中未观察到。在存在NADPH-细胞色素P-450还原酶、NADPH和磷脂的情况下,部分纯化的细胞色素P-450组分催化牛磺鹅去氧胆酸6α-羟基化的速率比微粒体高160倍。该细胞色素P-450组分不催化5β-胆甾烷-3α,7α-二醇或睾酮的6α-羟基化,也不催化胆固醇的7α-羟基化。