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ID 49982
本文ファイル
著者
NAKAI, Taketomi
キーワード
Cholesterol 7α-hydroxylase
Guinea pig
Cholesterol
NDC
医学
抄録(英)
Cholesterol 7α-hydroxylase (cholesterol, NADPH: oxygen oxidoreductase, 7α-xhydroxylating, EC 1.14.13.17), was partially purified from liver microsomes of guinea pig. The purified sample showed a specific activity of 1. 76 nmol/min/mg of protein and a turnover number of 2.3 nmol/min/nmol of cytochrome P-450, which were 100 times as high as respective values of microsomes. Cholesterol 7α-hydroxy lase activity was reconstituted from the partially purified cytochrome P-450, NADPH-cytochrome P-450 reductase, dilauroylglyceryl-3-phosphorylcholine and the NADPH generating system. The reconstituted system showed an absolute requirement for cytochrome P-450, NADPH-cytochrome P-450 reductase and NADPH. The apparent Km value for cholesterol in the reconstituted system was 33 μM and Vmax was 3.4 nmol/min/mg of protein. Cholesterol 7α-hydroxylase activity was significantly inactivated by iodoacetamide and p-chloromercuribenzoate, but not either by aminoglutethimide or by metyrapone.
掲載誌名
Hiroshima Journal of Medical Sciences
36巻
2号
開始ページ
227
終了ページ
231
出版年月日
1987-06
出版者
Hiroshima Journal Medical Press
ISSN
0018-2052
NCID
PubMedID
言語
英語
NII資源タイプ
紀要論文
広大資料タイプ
学内刊行物(紀要等)
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
publisher
部局名
医歯薬学総合研究科
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