Abstract
The cytochromes P-450 metabolize a diverse array of xenobiotic and endobiotic compounds, including carcinogens, drugs, and steroids (1-3). The different isozymes differ in their substrate and product specificities and reactivities. The types and amounts of isozymes in a tissue therefore regulate the metabolic conversion of substrates to products. Progress in understanding the role of individual P-450s in metabolism of specific substrates, and in relating P-450 phenotype to individual differences in sensitivity to drugs and carcinogens, has been hindered by the multiplicity of the P-450s. The approach we have taken to the multiplicity problem is to prepare and use monoclonal antibodies (MAbs) as specific probes to individual and epitope-specific classes of P-450s (4–6).
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© 1986 Plenum Press, New York
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Friedman, F.K., Park, S.S., Song, B.J., Cheng, K.C., Gelboin, H.V., Fujino, T. (1986). Monoclonal Antibody-Directed Analysis of Cytochrome P-450. In: Kocsis, J.J., Jollow, D.J., Witmer, C.M., Nelson, J.O., Snyder, R. (eds) Biological Reactive Intermediates III. Advances in Experimental Medicine and Biology, vol 197. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5134-4_11
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DOI: https://doi.org/10.1007/978-1-4684-5134-4_11
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