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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1987-7-14
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pubmed:abstractText |
The kinetic parameters of binding and hydroxylation of hydrophobic substrate 3,4-benzpyrene have been studied in liver microsomes of untreated and 3-methylcholanthrene treated mice. The reaction of benzpyrene-hydroxylase has been established to be described by hyperbolic curve, which characterizes the dependence of [ES] and d(P)/dt on [E0] for reactions in biphasic system. A key role of microsomal membraneous phospholipids has been revealed in competitive inhibition of 3,4-benzpyrene hydroxylation. For the adequate application of Michaelis--Menten theory for benzpyrene-hydroxylation reaction a modified method of 3,4-benzpyrene-hydroxylation in the samples with low content of protein in microsomal fraction is suggested.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0470-4606
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30-6
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pubmed:dateRevised |
2009-11-11
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pubmed:meshHeading |
pubmed-meshheading:3580418-Animals,
pubmed-meshheading:3580418-Benzo(a)pyrene,
pubmed-meshheading:3580418-Hydroxylation,
pubmed-meshheading:3580418-Kinetics,
pubmed-meshheading:3580418-Membrane Lipids,
pubmed-meshheading:3580418-Methylcholanthrene,
pubmed-meshheading:3580418-Mice,
pubmed-meshheading:3580418-Mice, Inbred C57BL,
pubmed-meshheading:3580418-Microsomes, Liver,
pubmed-meshheading:3580418-Phospholipids,
pubmed-meshheading:3580418-Protein Binding,
pubmed-meshheading:3580418-Spectrometry, Fluorescence
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pubmed:year |
1987
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pubmed:articleTitle |
[Kinetic characteristics of 3,4-benzpyrene hydroxylation in the liver microsomes of mice].
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pubmed:publicationType |
Journal Article,
Comparative Study,
English Abstract
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