Abstract:
:The cytochrome P-450 catalyzing 26-hydroxylation of C27-steroids (cytochrome P-450(26] was purified from rabbit liver mitochondria. The specific content of the cytochrome P-450 was 13.6 nmol per mg of protein and the 26-hydroxylase activity towards 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol was 31,300 pmol/nmol of cytochrome P-450 x min-1. The preparation also catalyzed 25-hydroxylation of vitamin D3 at a rate of 350 pmol/nmol of cytochrome P-450 x min-1. A monospecific monoclonal antibody raised against the 26-hydroxylating cytochrome P-450 was prepared. Experiments with the monoclonal antibody showed that cytochrome P-450(26) is susceptible to proteolytic degradation during purification unless the protease inhibitor TPCK is included in the buffers. After coupling to Sepharose the antibody was able to bind to cytochrome P-450(26) and to decrease the 26-hydroxylation of 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol. The 25-hydroxylation of vitamin D was not inhibited by the antibody. The results indicate that there are different species of cytochrome P-450 in rabbit liver mitochondria catalyzing 26-hydroxylation of 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol and 25-hydroxylation of vitamin D3. The N-terminal amino acid sequence of the cytochrome P-450(26) differed from those of hitherto isolated mammalian cytochromes P-450.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Dahlbäck Hdoi
10.1016/s0006-291x(88)80006-8subject
Has Abstractpub_date
1988-11-30 00:00:00pages
30-6issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(88)80006-8journal_volume
157pub_type
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