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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1978-2-18
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pubmed:abstractText |
The roles of type I binding and NADPH-cytochrome P-450 reductase in ethylmorphine demethylation were investigated in two strains of mice, using sex differences in these activities as a tool. In the CPB-SE strain, females metabolize ethylmorphine faster than males. Sex differences in cytochrome P-450 content and endogenous NADPH-cytochrome P-450 reductase activity were too small to account for this. On the other hand, the differences in the magnitudes of type I spectra and ethylmorphine-induced enhancement of cytochrome P-450 reduction were considerable larger than those in the rates of demethylation. All parameters, except endogenous cytochrome P-450 reduction, were modified in a similar way by testosterone pretreatment: in females they were depressed to the male level, whereas in males they remained unchanged. Castration had no effect in females and enhanced the activities in males. The CPB-V strain exhibited little or no sex differences in ethylmorphine demethylation, cytochrome P-450 content and endogenous cytochrome P-450 reduction. Testosterone pretreatment had little or no influence on these activities. Type I binding and reductase stimulation, however, showed sex differences, comparable to those observed in the CPB-SE strain, which were also abolished by testosterone. A relationship between reductase stimulation and type I binding was observed, which was, apparently, independent of sex or strain. It is concluded that androgen primarily influences the amount of cytochrome P-450-substrate complex formed, but that the reduction of this complex is not rate-limiting in the demethylation of ethylmorphine.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmorphine-N-Demethylase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, N-Demethylating,
http://linkedlifedata.com/resource/pubmed/chemical/Testosterone
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0009-2797
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-95
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:589699-Animals,
pubmed-meshheading:589699-Castration,
pubmed-meshheading:589699-Cytochrome P-450 Enzyme System,
pubmed-meshheading:589699-Cytochrome Reductases,
pubmed-meshheading:589699-Ethylmorphine-N-Demethylase,
pubmed-meshheading:589699-Female,
pubmed-meshheading:589699-Male,
pubmed-meshheading:589699-Mice,
pubmed-meshheading:589699-Mice, Inbred Strains,
pubmed-meshheading:589699-Microsomes, Liver,
pubmed-meshheading:589699-Oxidoreductases, N-Demethylating,
pubmed-meshheading:589699-Protein Binding,
pubmed-meshheading:589699-Sex Factors,
pubmed-meshheading:589699-Species Specificity,
pubmed-meshheading:589699-Testosterone
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pubmed:year |
1977
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pubmed:articleTitle |
Sex- and strain-dependent hepatic microsomal ethylmorphine N-demethylation in mice: the roles of type I binding and NADPH-cytochrome P-450 reductase.
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pubmed:publicationType |
Journal Article,
Comparative Study
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