Expression of bovine 17 alpha-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells
作者： M. Zuber , E. Simpson , M. Waterman
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摘要: Cortisol production requires the activity of only 17 alpha-hydroxylase, whereas formation sex steroids both alpha-hydroxylase and 17,20-lyase activities. Studies in reconstituted enzyme systems have suggested that a single steroid hydroxylase, cytochrome P-450 (P-450(17) alpha), catalyzes By expression bovine adrenocortical P-450(17 alpha) COS 1 (transformed monkey kidney) cells, which normally contain no detectable P-450(17) alpha, it has now been established situ polypeptide chain does catalyze reactions. This heterologous system supports alpha-hydroxylation pregnenolone progesterone with equal efficiency, but about five times as much when alpha-hydroxypregnenolone is substrate than alpha-hydroxyprogesterone substrate. For these activities to be observed newly synthesized apocytochrome alpha must bind heme insert into endoplasmic reticulum such endogenous reductase can support hydroxylation. Thus, cells are useful for study various forms P-450.
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