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Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.

The roles of different forms of cytochrome P-450 in activation and deactivation of toxic chemicals, 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...

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Detalles Bibliográficos
Autores principales: Stegeman, J J, Kloepper-Sams, P J
Formato: Texto
Lenguaje:English
Publicado: 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1474358/
https://www.ncbi.nlm.nih.gov/pubmed/3297668
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author Stegeman, J J
Kloepper-Sams, P J
author_facet Stegeman, J J
Kloepper-Sams, P J
author_sort Stegeman, J J
collection PubMed
description The roles of different forms of cytochrome P-450 in activation and deactivation of toxic chemicals, 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 monooxygenase 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 LM4b from trout, and cytochrome P-450c from cod have properties similar to each other and appear to be homologous hydrocarbon or BNF-inducible isozymes. Partially purified cytochrome DBA-P-450-I from little skate, Raja erinacea, is possibly an elasmobranch counterpart of these teleost forms. 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.
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spelling pubmed-14743582006-06-09 Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals. Stegeman, J J Kloepper-Sams, P J Environ Health Perspect Research Article The roles of different forms of cytochrome P-450 in activation and deactivation of toxic chemicals, 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 monooxygenase 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 LM4b from trout, and cytochrome P-450c from cod have properties similar to each other and appear to be homologous hydrocarbon or BNF-inducible isozymes. Partially purified cytochrome DBA-P-450-I from little skate, Raja erinacea, is possibly an elasmobranch counterpart of these teleost forms. 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. 1987-04 /pmc/articles/PMC1474358/ /pubmed/3297668 Text en
spellingShingle Research Article
Stegeman, J J
Kloepper-Sams, P J
Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title_full Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title_fullStr Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title_full_unstemmed Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title_short Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.
title_sort cytochrome p-450 isozymes and monooxygenase activity in aquatic animals.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1474358/
https://www.ncbi.nlm.nih.gov/pubmed/3297668
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