Ring-andN-hydroxylation of 2-acetamidofluorene by rat liver reconstituted cytochrome P-450 enzyme system.
Ring-andN-hydroxylation of 2-acetamidofluorene by rat liver reconstituted cytochrome P-450 enzyme system.
复制标题
大鼠肝脏重建细胞色素 P-450 酶系统对 2-乙酰氨基芴的环-和 N-羟基化。
DOI：
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发表时间：
1975
影响因子：
4.1
通讯作者：
Kathleen Zaleski
中科院分区：
文献类型：
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作者：
P. Lotlikar;Kathleen Zaleski
使用从对照大鼠和 3-甲基胆蒽预处理大鼠肝脏微粒体部分中重建的细胞色素 P-450 酶研究 2-乙酰氨基芴的 N-和环羟基化。蛋白酶处理和 Triton X-100 溶解是部分纯化细胞色素 P-450 组分的两个重要步骤。细胞色素 P-450 和 NADPH-细胞色素 c 还原酶组分都是最佳 N 羟基化和环羟基化活性所必需的。羟基化活性由细胞色素P-450级分的来源测定；来自预处理动物的细胞色素 P-450 级分比来自对照的级分活性高数倍。对照和预处理动物的重建系统形成的 N-羟基化代谢物大于其各自的完整微粒体部分。
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.