Abstract
Rat liver microsomal cytochrome P-450 d was abundantly expressed in the yeast Saccharomyces cerevisiae by using a yeast- Escherichia coli shuttle vector consisting of rat liver P-450 d cDNA and yeast acid phosphatase promoter. The expressed cytochrome P-450 d was immunologically crossed with rat liver P-450 d. The hydroxylase activity of estra-1,3,5(10)-triene-3,17β-diol was 11 nmol/min per nmol P-450 d, which is comparable to that reported previously for rat liver P-450 d. The expressed P-450 d content was nearly 1% of total yeast protein as estimated from immunoblotting, hydroxylase activity and optical absorption of the reduced CO form.
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