Faculty Publications
Purification And Characterization Of Steroid-Metabolizing Cytochrome P-450 Dependent Mixed Function Oxidase Systems From Bovine Adrenocortical Microsomes
Document Type
Book Chapter
Journal/Book/Conference Title
Microsomes, Drug Oxidations and Chemical Carcinogenesis
First Page
203
Last Page
206
Abstract
Cytochrome P-450 and NADPH cytochrome c (P-450) reductase were purified from bovine adrenocortical (BAC) microsomes. Cytochrome P-450 AM-1 purified to 10–12 nanomoles P-450/mg protein by AM 2 SO 4 fractionation and hydrophobic interaction chromatography showed essentially one band by SDS-page (> 95%) with a MW= 52,000. Fraction P-450 AM-2 with a specific content of 3-4 nanomoles P-450/mg protein contained two hemeproteins with MW of 49,000 and 52,000. Partially purified reductase reduced cytochrome P-450. Adrenodoxin was not required nor did it stimulate reduction. Photoaffinity labeling studies show the inhibitor derived label 1-(4-azidophenyl) imidazole to have high affinity for BAC microsomal P-450. Labeling experiments using partially purified BAC microsomal P-450 afforded stoichiometric label incorporation.
Original Publication Date
1-1-1980
DOI of published version
10.1016/B978-0-12-187701-9.50041-3
Recommended Citation
Bumpus, J. A.; Obidoa, O.; and Dus, K. M., "Purification And Characterization Of Steroid-Metabolizing Cytochrome P-450 Dependent Mixed Function Oxidase Systems From Bovine Adrenocortical Microsomes" (1980). Faculty Publications. 6636.
https://scholarworks.uni.edu/facpub/6636
