Imaoka S, Funae Y
Biochem Biophys Res Commun. 1986 Dec 15;141(2):711-7. doi: 10.1016/s0006-291x(86)80230-3.
The major form of cytochrome P-450, P-450K-5, was purified from kidney microsomes of untreated male rats with high-performance liquid chromatography with anion-exchange and hydroxylapatite columns. The monomeric molecular weight of P-450K-5 was 52000 on SDS-polyacrylamide gel electrophoresis and the CO-reduced absorption maximum was at 452 nm. P-450K-5 catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was inefficient in the N-demethylation of benzphetamine and the O-dealkylation of 7-ethoxycoumarine. The NH2-terminal sequence of P-450K-5 was quite different from cytochrome P-450s purified from rat hepatic microsomes.
细胞色素P-450的主要形式，即P-450K-5，通过使用阴离子交换柱和羟基磷灰石柱的高效液相色谱法，从未经处理的雄性大鼠的肾微粒体中纯化得到。在SDS-聚丙烯酰胺凝胶电泳上，P-450K-5的单体分子量为52000，一氧化碳还原吸收最大值在452nm处。P-450K-5催化月桂酸的ω-和（ω-1）-羟基化反应，但在苄非他明的N-脱甲基反应和7-乙氧基香豆素的O-脱烷基反应中效率较低。P-450K-5的NH2末端序列与从大鼠肝微粒体中纯化得到的细胞色素P-450有很大不同。
