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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| File | |
| 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.
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| 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
|
