大鼠肝脏重组细胞色素P-450酶系统对2-乙酰氨基芴的环化和N-羟基化作用。
Ring-andN-hydroxylation of 2-acetamidofluorene by rat liver reconstituted cytochrome P-450 enzyme system.
作者信息
Lotlikar P D, Zaleski K
出版信息
Biochem J. 1975 Sep;150(3):561-4. doi: 10.1042/bj1500561.
Abstract
The N- and ring-hydroxylation of 2-acetamidofluorene were studied with a reconstituted cytochrome P-450 enzyme from microsomal fractions of liver from both control and 3-methylcholanthrene-pretreated rats. Proteinase treatment and Triton X-100 solubilization were two important steps for partial purification of the cytochrome P-450 fraction. Both cytochrome P-450 and NADPH-cytochrome c reductase fractions were required for optimum N- and ring-hydroxylation activity. Hydroxylation activity was determined by the source of cytochrome P-450 fraction; cytochrome P-450 fraction from pretreated animals was severalfold more active than the fraction from controls. Formation of N-hydroxylated metabolites with reconstituted systems from both control and pretreated animals was greater than that with their respective whole microsomal fractions.
摘要
利用来自对照大鼠和经3-甲基胆蒽预处理大鼠肝脏微粒体部分的重组细胞色素P-450酶，研究了2-乙酰氨基芴的N-羟基化和环羟基化反应。蛋白酶处理和 Triton X-100增溶是细胞色素P-450部分纯化的两个重要步骤。细胞色素P-450和NADPH-细胞色素c还原酶部分对于最佳的N-羟基化和环羟基化活性都是必需的。羟基化活性取决于细胞色素P-450部分的来源；来自预处理动物的细胞色素P-450部分的活性比来自对照动物的部分高几倍。用对照动物和预处理动物的重组系统形成的N-羟基化代谢产物比用它们各自的完整微粒体部分形成的更多。
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