Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference24 articles.
1. Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes
2. Phosphatidylcholine Requirement in the Enzymatic Reduction of Hemoprotein P-450 and in Fatty Acid, Hydrocarbon, and Drug Hydroxylation
3. Preparation and Properties of Partially Purified Cytochrome P-450 and Reduced Nicotinamide Adenine Dinucleotide Phosphate-Cytochrome P-450 Reductase from Rabbit Liver Microsomes
4. Cytochrome P-450 purified to apparent homogeneity from phenobarbital-induced rabbit liver microsomes: Catalytic activity and other properties
5. Resolution of the Cytochrome P-450-containing ω-Hydroxylation System of Liver Microsomes into Three Components
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