Partial Purification and Characterization of Cholesterol 7α-Hydroxylase from Guinea Pig

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