[21] Purification from rabbit and rat liver of cytochromes P-450 involved in bile acid biosynthesis
- 1 January 1985
- book chapter
- Published by Elsevier
- Vol. 111, 364-377
- https://doi.org/10.1016/s0076-6879(85)11023-2
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids.Journal of Biological Chemistry, 1984
- Hydroxylations in Biosynthesis of Bile Acids. Cytochrome P-450 LM4 and 12alpha-Hydroxylation of 5beta-Cholestane-3alpha,7alpha-diolEuropean Journal of Biochemistry, 1982
- Properties of Reconstituted Cholesterol 7α‐Hydroxylase System from Rat and Rabbit Liver MicrosomesEuropean Journal of Biochemistry, 1979
- Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography.Journal of Biological Chemistry, 1976
- Side chain hydroxylations in biosynthesis of cholic acid. 25- and 26-Hydroxylation of 5beta-cholestane-3alpha, 7alpha, 12alpha-triol by reconstituted systems from rat liver microsomes.Journal of Biological Chemistry, 1976
- Bile Acid MetabolismAnnual Review of Biochemistry, 1975
- ω‐Hydroxylation of Steroid Side‐Chain in Biosynthesis of Bile AcidsEuropean Journal of Biochemistry, 1973
- Studies on Adrenal Steroid HydroxylasesJournal of Biological Chemistry, 1973
- Adrenal steroid hydroxylases. Oxidation- reduction properties of adrenal iron-sulfur protein (adrenodoxin)Biochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970