skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals

Journal Article · · Environ. Health Perspect.; (United States)
DOI:https://doi.org/10.1289/ehp.877187· OSTI ID:6785991

The roles of different forms of cytochrome P-450 in activation and deactivation of toxic chemicals, such as benzopyrene synthesis and breakdown of steroid hormones, and other functions, indicate the significance of these enzymes. Monooxygenase systems have been studied in species from several phyla of aquatic organisms. However, cytochrome P-450, the dominant catalyst in xenobiotic monoxygenase activity, is best studied in fish. Forms of cytochrome P-450 have been purified from several teleost species, including scup (Stenotomus chrysops), rainbow trout (Salmo gairdneri), and cod (Gadus morhua). Cytochrome P-450E from scup, cytochrome P-450 LM/sub 4b/ from trout, and cytochrome P-450c from cod have properties similar to each other and appear to be homologous hydrocarbons or BNF-inducible isozymes. Cytochrome P-450E from scup is immunochemically related to the major BNF-inducible isozyme (cytochrome P-450c or BNF-B) in rats, indicating homology between the fish and mammalian BNF-inducible isozymes. Several other cytochrome P-450 forms with interesting or unusual properties have been purified from aquatic species. Mammalian homologs are not yet known for these isozymes. Further studies of cytochrome P-450 forms in aquatic species should establish additional homologies and the regulation of these forms by chemical and biological variables, possibly providing fundamental insights into the function and evolution of these proteins.

Research Organization:
Woods Hole Oceanographic Institution, MA
OSTI ID:
6785991
Journal Information:
Environ. Health Perspect.; (United States), Vol. 71
Country of Publication:
United States
Language:
English