膜结合型甲基胆蒽诱导细胞色素P-450的催化活性。
Catalytic activity of the membrane-bound methylcholanthrene-inducible cytochrome P-450.
作者信息
Mishin V M, Lyakhovich V V
出版信息
FEBS Lett. 1985 Jan 1;179(1):74-6. doi: 10.1016/0014-5793(85)80194-0.
PMID:3965304
Abstract
The benzopyrene hydroxylase activity of the methylcholanthrene-inducible form of cytochrome P-450 (P-448) has been studied in native and reconstituted liver microsomal membranes. The data obtained show that the molecular catalytic activity of membrane-bound cytochrome P-448 depends on the molar ratio of the cytochrome to NADPH-cytochrome P-450 reductase and that the optimal ratio for maximal activity of cytochrome P-448 in the microsomal membrane essentially differs from the equimolar one.
摘要
在天然和重组肝微粒体膜中，对甲基胆蒽诱导型细胞色素P - 450（P - 448）的苯并芘羟化酶活性进行了研究。所得数据表明，膜结合细胞色素P - 448的分子催化活性取决于细胞色素与NADPH - 细胞色素P - 450还原酶的摩尔比，并且微粒体膜中细胞色素P - 448最大活性的最佳比例与等摩尔比例基本不同。
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