Fu F H, Sun M J
Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, China.
Zhongguo Yao Li Xue Bao. 1990 Mar;11(2):123-6.
In our preliminary study, it has been found that VX oxidase exists in the microsome fraction of rat liver and the catalytic reaction needs the participation of molecular oxygen and coenzyme I or II. In this paper, the data showed that deoxycholate inactivated both the mixed function oxidase and VX oxidase. The specific inhibitor proadifen of the mixed function oxidase also profoundly inhibited VX oxidase activity. The complex of VX and cytochrome P-450 exhibited typical difference spectrum of type I. Aniline competitively inhibited the inactivation of VX catalyzed by microsomes. These results indicate that VX is one of the substrates of mixed function oxidase. VX oxidase in the rat liver cells is exactly the mixed function oxidase.
在我们的初步研究中,已发现VX氧化酶存在于大鼠肝脏的微粒体部分,其催化反应需要分子氧和辅酶I或II的参与。本文数据表明,脱氧胆酸盐使混合功能氧化酶和VX氧化酶均失活。混合功能氧化酶的特异性抑制剂丙胺太林也显著抑制VX氧化酶活性。VX与细胞色素P-450的复合物呈现出典型的I型差光谱。苯胺竞争性抑制微粒体催化的VX失活。这些结果表明,VX是混合功能氧化酶的底物之一。大鼠肝细胞中的VX氧化酶正是混合功能氧化酶。