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Antibodies as Probes of Cytochrome P450 Isozymes

  • Paul E. Thomas
  • Linda M. Reik
  • Sarah L. Maines
  • Stelvio Bandiera
  • Dene E. Ryan
  • Wayne Levin
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 197)

Abstract

Cytochrome P450*, an integral membrane protein, is widely distributed in many mammalian tissues, but is present in the highest concentration in hepatic endoplasmic reticulum. It functions as the terminal oxidase of an electron transport system that is involved in the metabolism of a large number of xenobiotics as well as endogenous substrates such as steroids, bile acids, fatty acids and prostaglandins (1). Although this enzyme system formerly was believed to function principally in detoxification, it is now known to metabolically activate many compounds to reactive metabolites that initiate toxic and carcinogenic events (2). Even more interesting is the observation that only certain optical isomers of bay-region diol epoxides of polycyclic aromatic hydrocarbons are carcinogenic, and that the cytochrome P450-dependent mixed function oxidase system preferentially catalyzes the formation of the optical isomer with the highest carcinogenic activity (3).

Keywords

Epoxide Hydrolase Microsomal Cytochrome Distinct Epitope Cytochrome P450 Isozyme Hepatic Microsomal Cytochrome 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Paul E. Thomas
    • 1
  • Linda M. Reik
    • 1
  • Sarah L. Maines
    • 1
  • Stelvio Bandiera
    • 1
  • Dene E. Ryan
    • 1
  • Wayne Levin
    • 1
  1. 1.Laboratory of Experimental Carcinogenesis and Metabolism Roche InstituteMolecular BiologyNutleyUSA

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