1. Inhibition of a purified adrenal steroid 21-hydroxylating system by cytochrome P-450 particles
- Author
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Joyce E. Mandel and Charles Matthijssen
- Subjects
Male ,Cytochrome ,CYP1B1 ,Clinical Biochemistry ,25-Hydroxyvitamin D3 1-alpha-hydroxylase ,Mitochondria, Liver ,Biochemistry ,Mixed Function Oxygenases ,Electron Transport Complex IV ,Endocrinology ,Microsomes ,Adrenal Glands ,Hydroxyprogesterones ,Animals ,Cytochrome c oxidase ,Steroid 11-beta-hydroxylase ,Molecular Biology ,Pharmacology ,Sheep ,biology ,Chemistry ,Cytochrome c ,Organic Chemistry ,Cytochrome P450 reductase ,Mitochondria ,Liver ,Spectrophotometry ,CYP17A1 ,biology.protein ,Cytochromes ,Rabbits - Abstract
Studies with a preparation of an adrenal steroid 21-hydroxylating system exhibiting activity in the absence of cytochrome P-450 have been extended. In contrast to the adrenal 11-hydroxylating system, in which cytochrome P-450 acts as the terminal oxidase, it was found that cytochrome P-450 in the form of cytochrome P-450 particles inhibits the conversion of 17-hydroxyprogesterone * to 17,21-dihydroxyprogesterone under our experimental conditions.
- Published
- 1970
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