Abstract
The steroid 21-hydroxylase system was purified from bovine adrenocortical microsomes. The physicochemical properties of the cytochrome P-450 s21 were studied. The properties of NADPH-cytochrome P-450 reductase (EC 1.6.2.4) of bovine adrenocortical microsomes have been reported previously (Hiwatashi, A. and Ichikawa, Y. (1979) Biochim. Biophys. Acta 580, 44–63). The steroid 21-hydroxylase system was reconstituted by cytochrome P-450 s21 and NADPH-cytochrome P-450 reductase in the presence of detergent. The substrate specificity of the cytochrome P-450 s21 was examined with the reconstituted system. The enzyme system was active in the 21-hydroxylations of 17 α- hydroxyprogesterone and progesterone, and the N-demethylation of (+)-benzphetamine. The cytochrome P-450 s21 purified to as high as 16–17 nmol per mg protein was an electrophoretically pure glycoprotein. The molecular weight of the cytochrome P-450 s21 was estimated to be 47 500 by SDS-polyacrylamide gel electrophoresis. Although cytochrome P-450 scc or cytochrome P-450 11β of bovine adrenocortical mitochondria did not react with antibody to cytochrome P-450 BPA of bovine liver microsomes, the cytochrome P-450 s21 formed an immunoprecipitin line against the antibody to cytochrome P-450 BPA in the Ouchterlony double diffusion test.
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