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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1979-3-24
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pubmed:abstractText |
In the presence of hepatic microsomes, styrene produced a type I difference spectrum, which demonstrates that styrene binds to the catalytic site of ferricytochrome P-450. A comparison of the binding parameters for the interaction of styrene with noninduced, phenobarbital-induced, and 3-methylcholanthrene-induced microsomes indicated that styrene is predominantly bound by cytochrome P-450 and not by cytochrome P-448. Inhalation exposure to a mixture of acetone (1,000 ppm, 6 h/d) and styrene (300 ppm, 6 h/d) for 5 d caused a distinct decrease in hepatic free nonprotein sulfhydryl groups. This decrease could be observed both with and without phenobarbital treatment. Acetone inhalation alone also enhanced ethoxycoumarin O-deethylase activity in rats without pretreatments. Acetone inhalation also increased the cytochrome P-450 content of liver microsomes, but it had no effect on NADPH cytochrome c reductase or epoxide hydratase activity. Combined exposure to styrene and acetone enhanced NADPH cytochrome c reductase activity in nonphenobarbital-treated rats, but no effect was seen in the phenobarbital-treated animals. Phenobarbital treatment of animals can greatly modify the biotransformation and toxicity of styrene, phenobarbital inducible P-450 hemoprotein playing a predominant role in its metabolism. Simultaneous inhalation exposure to acetone also interacts with the metabolism of styrene.
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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/Acetone,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Methylcholanthrene,
http://linkedlifedata.com/resource/pubmed/chemical/Phenobarbital,
http://linkedlifedata.com/resource/pubmed/chemical/Styrenes,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
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pubmed:status |
MEDLINE
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pubmed:issn |
0355-3140
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4 Suppl 2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-52
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:734416-Acetone,
pubmed-meshheading:734416-Animals,
pubmed-meshheading:734416-Binding Sites,
pubmed-meshheading:734416-Biotransformation,
pubmed-meshheading:734416-Cytochrome P-450 Enzyme System,
pubmed-meshheading:734416-Drug Interactions,
pubmed-meshheading:734416-Endoplasmic Reticulum,
pubmed-meshheading:734416-Glutathione,
pubmed-meshheading:734416-Male,
pubmed-meshheading:734416-Methylcholanthrene,
pubmed-meshheading:734416-Microsomes, Liver,
pubmed-meshheading:734416-Phenobarbital,
pubmed-meshheading:734416-Rats,
pubmed-meshheading:734416-Styrenes,
pubmed-meshheading:734416-Sulfhydryl Compounds
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pubmed:year |
1978
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pubmed:articleTitle |
Interaction of styrene and acetone with drug biotransformation enzymes in rat liver.
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pubmed:publicationType |
Journal Article
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