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Molecular Pharmacology, Vol 11, 201-210, Copyright © 1975 by the American Society for Pharmacology and Experimental Therapeutics

Reconstituted Liver Microsomal Enzyme System That Hydroxylates Drugs, Other Foreign Compounds, and Endogenous Substrates

VIII. Different Catalytic Activities of Rabbit and Rat Cytochromes P-448

JOSEPH C. KAWALEK 1 and ANTHONY Y. H. LU 1

1 Department of Biochemistry and Drug Metabolism, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110

Cytochrome P-448 was partially purified from 3-methylcholanthrene-treated rabbits to a specific content of 9-10 nmoles of cytochrome P-448 per milligram of protein. This partially purified rabbit cytochrome P-448 was only 10% as active as rat cytochrome P-448 in catalyzing the hydroxylation of benzo[a]pyrene in the presence of NADPH-cytochrome c reductase and lipid. Hydroxylation of benzo[a]pyrene supported by the rabbit P-448 fraction was much more susceptible to inhibition by 7,8-benzoflavone and diethylaminoethyldiphenylpropyl acetate (SKF 525-A) than was the corresponding P-448 from rat. These results suggest that rabbit cytochrome P-448 is catalytically different from rat cytochrome P-448.

Note:
ACKNOWLEDGMENT We thank Mrs. Margaret Althoff for assistance in preparing the manuscript.

Submitted on September 30, 1974






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