Metabolism of 32-Hydroxylated 24,25-Dihydrolanosterols by Partially Purified Cytochrome P-450_<14DM> from Rat Liver Microsomes
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概要
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Metabolism of 32-hydroxylated 24,25-dihydrolanosterols (1-3), including the intermediate of lanosterol and 24,25-dihydrolanosterol (4,DHL) demethylation, were studied in a reconstituted system consisting of rat liver partially purified cytochrome P-450,which catalyzes lanosterol 14-demethylation (cytochrome P-450_<14DM>), and reduced nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome P-450 reductase. The reconstituted system converted lanost-8-ene-3β, 32-diol (1) to 4,4-dimethyl-5α-cholesta-8,14,dien-3β-ol (5), the 14-dehydroxymethylated product, in the same way as 4. Lanost-7-ene-3β-32-diol (2) and lanost-6-ene-3β, 32-diol (3), the isomers of 1,were not converted to the corresponding 14-dehydroxymethylated products. The apparent K_m value of cytochrome P-450_<14DM> for 1 was about 1/6 of that for 4. The metabolism of 4 was inhibited by 7-oxo-24,25-dihydrolanosterol (6,7-oxo-DHL), which is a potent inhibitor of cholesterol biosynthesis from lanosterol or 4. However, the metabolism of 1 was less inhibited by 6 than that of 4.
- 公益社団法人日本薬学会の論文
- 1988-08-25
著者
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佐藤 美洋
北海道大学大学院薬学研究院
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佐藤 良博
共立薬科大学名誉
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園田 よし子
Kyoritsu College of Pharmacy
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佐藤 良博
Kyoritsu College of Pharmacy
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関川 善夫
Department Of Pharmaceutical Sciences National Institute Of Public Health
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佐藤 良博
共立薬大
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Sato Y
(present Address)tsukuba Research Institute Banyu Pharmaceutical Co. Ltd.
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関川 善夫
Kyoritsu College of Pharmacy
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佐藤 嘉信
Department Of Chemical Engineering University Of Osaka Prefecture
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