Abstract
Monoclonal hydribomas which produce antibodies against human liver microsomal cytochrome P-450 were developed. Three similar hybridomas produced antibodies which recognized an epitope specific to a family of human P-450 isozymes (P-450 5). This epitope was also present on cytochrome P-450 PCN-E (pregnenolone-16α-carbonitrile induced) from rat liver microsomes, but this isozyme differed from the human P-450 5 by its molecular weight. These antibodies enabled us to quantify cytochrome P-450 5 in human liver microsomes and to demonstrate an important quantitative polymorphism in the human liver monooxygenase system.
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