Abstract
Rabbit liver microsomes were either solubilised by sodium cholate-sonication treatment and a protein fraction precipitated at 45% saturation with ammonium sulfate, or first washed with acetone, solubilised by sodium deoxycholate-sonication treatment and precipitated at 40–80% saturation. The 45% fraction, which contained cytochrome P-450, retained the C-21 and C-6-hydroxylase activity of the original microsomes when incubated with progesterone in the presence of NADPH and air. Inhibition of the cytoehrome P-450 with carbon monoxide had no effect on steroid hydroxylation. The 40–80% fraction was free of detectable cytochrome P-450 but actively metabolised progesterone to 6α-hydroxy progesterone. These results provide further evidence against the involvement of the cytochrome P-450 system in the C-21- and C-6-hydroxylation of progesterone by rabbit liver microsomes.
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