Purification and reconstitution of the cytochrome P-450 monooxygenase system from uninduced mouse liver
β Scribed by Patricia E. Levi; Ernest Hodgson
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 574 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0020-711X
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NADPH:cytochrome c (cytochrome P-450) reductase (Fp) from hamster liver microsomes has been purified to near homogeneity using a simple and rapid method. Microsomes were treated with the detergent Chaps (3-[(3-cholamidopropyl)dimethylammonio]propanesulfonic acid) in combination with 0.07% protamine
NADPH-cytochrome P450 reductase was purified to electrophoretic homogeneity from detergent-solubilized liver microsomes from the leaping mullet (Liza saliens). The purified reductase was characterized with respect to spectral, electrophoretic, and biocatalytic properties. In addition, effects of pH,