Metabolism of 32-Oxo-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-oxo-24,25-dihydrolanosterols (3β-hydroxylanost-8-en-32-al (4,Δ^8-CHO) and 3β-hydroxylanost-7-en-32-al (5,Δ^7-CHO)) was studied in a reconstituted system consisting of rat liver partially purified cytochrome P-450,which catalyzes lanosterol 14-demethylation (P-450_<14DM>), and reduced nicotineamide adenine dinucleotide phosphate (NADPH)-cytochrome P-450 reductase. The reconstituted system converted Δ^8-CHO (4) to 4,4-dimethyl-5α-cholesta-8,14-dien-3β-ol (2,8,14-Diene), which corresponds to the 14-deformylated product. Δ^7-CHO (5), the isomer of Δ^8-CHO (4), was not converted to the corresponding 14-deformylated product. The apparent K_m value of cytochrome P-450_<14DM> for Δ^8-CHO (4) was about 1/20 of that for 24,25-dihydrolanosterol (1,DHL). The metabolism of Δ^8-CHO (4) was inhibited by 7-oxo-24,25-dihydrolanosterol (6,7-oxo-DHL), which is a potent inhibitor of cholesterol biosynthesis from lanosterol or DHL (1). However, the metabolism of Δ^8-CHO (4) was less inhibited by 7-oxo-DHL (6) than that of DHL (1).
- 公益社団法人日本薬学会の論文
- 1989-10-25
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
Osaka Prefecture University
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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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