Abstract
Cytochrome P-450 supporting steroid 11β hydroxylase activity (cyt P-450 11β) was purified from bovine adrenal cortex mitochondria using a procedure, which included an octyl-sepharose adsorption step and elution of the protein in the presence of phosphatidyl-choline. Purified cyt P-450 11β could then be included into phosphatidyl choline-phosphatidyl ethanolamine (1 : 1) spherical vesicles (20–50 nm in diameter) during their formation upon gel filtration, as demonstrated by the protein refractoriness to trypsin hydrolysis. After inclusion into the phospholipid vesicles, cyt P-450 11β remained stable and expressed full 11β hydroxylase activity in a reconstituted system including purified adrenodoxin and adrenodoxin reductase.
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