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 (M(r) = 45000) exhibited 17,20-lyase activity of 6.78 nmol of androstenedione/min/nmol P-450, on incubation with 17 alpha-hydroxyprogesterone as a substrate. The other P-450 (M(r) = 46,000) exhibited no 17,20-lyase activity. Both P-450s exhibited 17 alpha-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 17 alpha-hydroxyprogesterone.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kuwada M,Takizawa N,Sone Ydoi
10.1006/bbrc.1996.0094subject
Has Abstractpub_date
1996-01-17 00:00:00pages
524-9issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(96)90094-7journal_volume
218pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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