Lotlikar P D, Baldy W J, Dwyer E N
Biochem J. 1975 Dec;152(3):705-8. doi: 10.1042/bj1520705.
Oxidative demethylation of dimethylnitosamine was studied with both reconstituted and unresolved liver microsomal cytochrome P-450 enzyme systems from rats and hamsters. Proteinase treatment of liver microsomal preparations yielded cytochrome P-450 particulate fractions. Both cytochrome P-450 and NADPH- cytochrome c reductase fractions were required for optimum demethylation activity. Particulate cytochrome P-450 fractions were more effecient than either Triton X-100- or cholatesolubilized preparations of these particles in demethylation activity with rat and hamster liver preparations appear to be due to differences in specificity in their cytochrome P-450 fractions.
利用大鼠和仓鼠的重组及未分离的肝微粒体细胞色素P - 450酶系统研究了二甲基亚硝胺的氧化脱甲基作用。用蛋白酶处理肝微粒体制剂可得到细胞色素P - 450颗粒部分。最佳脱甲基活性需要细胞色素P - 450和NADPH - 细胞色素c还原酶部分。在大鼠和仓鼠肝脏制剂的脱甲基活性方面,颗粒细胞色素P - 450部分比这些颗粒的Triton X - 100或胆酸盐溶解制剂更有效,这似乎是由于它们细胞色素P - 450部分的特异性差异所致。