Abstract
Two P-450s from adult pig testis were purified to specific contents of 11.2 and 12.0 nmol P-450/mg protein and shown to have minimum molecular weights of 45,000 and 46,000, respectively. The absorption spectra were typical of P-450s. The P-450s were separated from the two fractions by CM-C50 Sephadex column chromatography. One P-450 (Mr = 45000) exhibited 17,20-lyase activity of 6.78 nmol of androstenedione/min/nmol P-450, on incubation with 17α-hydroxyprogesterone as a substrate. The other P-450 (Mr = 46,000) exhibited no 17,20-lyase activity. Both P-450s exhibited 17α-hydroxylase activity that amounted to 10 nmol of steroid products. Accordingly, the two molecular species of P-450 are thus markedly different in 17,20-lyase activity toward 17α-hydroxyprogesterone.
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