Partial Purification and Characterization of Cholesterol 7α-Hydroxylase from Guinea Pig
Hiroshima Journal of Medical Sciences Volume 36 Issue 2
Page 227-231
published_at 1987-06
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Title ( eng ) |
Partial Purification and Characterization of Cholesterol 7α-Hydroxylase from Guinea Pig
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Creator |
NAKAI Taketomi
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Source Title |
Hiroshima Journal of Medical Sciences
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Volume | 36 |
Issue | 2 |
Start Page | 227 |
End Page | 231 |
Journal Identifire |
[PISSN] 0018-2052
[EISSN] 2433-7668
[NCID] AA00664312
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Abstract |
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.
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Keywords |
Cholesterol 7α-hydroxylase
Guinea pig
Cholesterol
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NDC |
Medical sciences [ 490 ]
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Language |
eng
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Resource Type | departmental bulletin paper |
Publisher |
Hiroshima Journal Medical Press
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Date of Issued | 1987-06 |
Publish Type | Version of Record |
Access Rights | open access |
Source Identifier |
[ISSN] 0018-2052
[NCID] AA00664312
[PMID] 3115919
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