ブタ副腎ミクロソームよりNicotineamide Adenine Dinucleotide Phosphate-チトクロームP-450還元酵素の精製と17α-ヒドロキシラーゼ, C_<17,20>リアーゼおよび21-ヒドロキシラーゼ活性の再構成

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Nicotineamide adenine dinucleotide phosphate-cytochrome P-450 reductase from porcine adrenal microsomes was purified to specific activity of 51.8 μmol/min/mg protein for cytochrome c reduction. The purified cytochrome P-450 reductase was a single protein band with a molecular weight of 78000±1000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The absorption spectrum of visible reagion showed peaks at 382 and 456 nm with a shoulder at 480 nm. The cytochrome P-450 reductase was capable of reconstituting 17α-hydroxylase, C_<17,20> lyase and 21-hydroxylase activities in the presence of adrenal microsomal cytochromes P-450. It was noticed that 21-hydroxylase activity for 17α-hydroxyprogesterone was 1.3 fold higher than that for progesterone, and 17α-hydroxylase activity was 2.4 fold higher than C_<17,20> lyase activity. The activity of 21-hydroxylase was 4-5 fold higher than 17α-hydroxylase activity when progesterone was used as a substrate. These activities catalyzed with cytochromes P-450 increased as a function of the amount of cytochrome P-450 reductase, and then these activities were saturated with P-450 reductase at the same ratio of reductase to P-450,i.e. 1 nmol of reductase/nmol of P-450.
公益社団法人日本薬学会の論文
1984-02-25