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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1988-3-2
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pubmed:abstractText |
The oxidative demethylation of the model substrate ethylmorphine has been characterized for the first time in the liver of a fish (Poecilia reticulata). The enzyme showed maximal activity at 35 degrees C and pH values higher than 8. The values of Km and Vmax for the reaction were 0.83 +/- 0.11 mM and 4.64 +/- 0.81 nmol HCHO/(mg microsomal protein) per min. The activity is attributed to the cytochrome P-450-dependent monoxygenase system, since it is inhibited by CO and requires NADPH; moreover it is inhibited competitively by alpha-naphthoflavone and non-competitively by metyrapone. The enzyme activity is induced by a two-week treatment of fish with phenobarbital and may be associated with a protein band of Mr 54,000.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0305-0491
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
619-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3427906-Animals,
pubmed-meshheading:3427906-Benzoflavones,
pubmed-meshheading:3427906-Cyprinodontiformes,
pubmed-meshheading:3427906-Enzyme Induction,
pubmed-meshheading:3427906-Ethylmorphine-N-Demethylase,
pubmed-meshheading:3427906-Female,
pubmed-meshheading:3427906-Kinetics,
pubmed-meshheading:3427906-Metyrapone,
pubmed-meshheading:3427906-Microsomes, Liver,
pubmed-meshheading:3427906-Oxidoreductases, N-Demethylating,
pubmed-meshheading:3427906-Phenobarbital,
pubmed-meshheading:3427906-Poecilia
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pubmed:year |
1987
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pubmed:articleTitle |
Xenobiotic-metabolizing enzyme systems in test fish--II. The ethylmorphine N-demethylase activity of guppy (Poecilia reticulata) liver.
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pubmed:affiliation |
Istituto Superiore di Sanità, Department of Comparative Toxicology and Ecotoxicology, Roma, Italy.
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pubmed:publicationType |
Journal Article
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