Back to Search
Start Over
[Partial purification and characterization of delta 7-sterol 5-desaturase from rat liver microsomes].
- Source :
-
[Hokkaido igaku zasshi] The Hokkaido journal of medical science [Hokkaido Igaku Zasshi] 1984 Jul; Vol. 59 (4), pp. 439-45. - Publication Year :
- 1984
-
Abstract
- The terminal oxygenase of the NADH-depending lathosterol (cholest-7-en-3 beta-ol) 5-desaturase system was partially purified from rat liver microsomes, by Triton X-100 solubilization, DEAE-cellulose column chromatography, and hydrophobic affinity chromatography with Aminohexyl-Sepharose. The terminal oxygenase activity was approximately 18 fold greater than the starting microsome, and the yield was 18.4%, nevertheless, the terminal enzyme activity was almost free from other electron transfer components in microsomes. It was demonstrated that NADH, molecular oxygen, phospholipid, and three enzymes: NADH-cytochrome b5 reductase, cytochrome b5, and the terminal oxygenase, were absolutely essential for lathosterol 5-desaturation in the reconstituted system. Furthermore, the rate of the NADH-depending lathosterol 5-desaturation in the reconstitution system, was proportional to the concentration either of the terminal desaturase, cytochrome b5, or NADH-cytochrome b5 reductase, under conditions in which other enzymes were present in excess.
Details
- Language :
- Japanese
- ISSN :
- 0367-6102
- Volume :
- 59
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- [Hokkaido igaku zasshi] The Hokkaido journal of medical science
- Publication Type :
- Academic Journal
- Accession number :
- 6489918