Journal of Biological Chemistry
A scheme is presented for the simultaneous isolation of P-45017n, and P-450c-21 from bovine adrenocortical microsomes and for their purification to specific contents of 19-20 nmol of P-450/mg of protein. Although cholate solubilized only 75% of the total amount of P- 450 and 36% of the NADPH-cytochrome C (P-450) reductase present in bovine adrenocortical microsomes as compared to Triton N-101, it produced a less complex mixture of microsomal proteins from which most of the P-450 could be removed by a 0-25% cut with polyethylene glycol. The P-450 fraction was subsequently resolved into individual P-450s by column chromatography on w-aminooctyl-Sepharose; these were then purified to homogeneity by a series of final chromatography steps including DEAE-, CM-, and w-aminooctyl-Sepharose.
Original Publication Date
DOI of published version
UNI ScholarWorks, Rod Library, University of Northern Iowa
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Bumpus, J. and Dus, K. M., "Bovine adrenocortical microsomal hemeproteins P-45017 alpha and P-450C-21. Isolation, partial characterization, and comparison to P-450SCC." (1982). Faculty Publications. 5526.