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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1984-12-20
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pubmed:abstractText |
The oxidation of benzo(a)pyrene (BP) by horseradish peroxidase (HRP) (EC 1.11.1.7) was examined spectrophotometrically by the decomposition of peroxidase-H2O2 intermediate "compound II." The rate constant of the oxidation of BP was 9.5 X 10(4) M-1 sec-1. The oxidation of BP by HRP was inhibited at high BP concentrations, and the hydrogen donor (BP) inhibition constant, KA', was 1.48 microM. The association constant, Kassoc, of the formation of a complex of BP and HRP at 403 nm was 4.37 X 10(4) M-1. The oxidation products of BP have been identified as 1,6-, 3,6- and 6,12-quinone BP. These products showed no mutagenicity in the mutagenicity assay.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0305-7232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
213-29
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6488152-Benzo(a)pyrene,
pubmed-meshheading:6488152-Horseradish Peroxidase,
pubmed-meshheading:6488152-Hydrogen Peroxide,
pubmed-meshheading:6488152-Kinetics,
pubmed-meshheading:6488152-Oxidation-Reduction,
pubmed-meshheading:6488152-Peroxidases,
pubmed-meshheading:6488152-Spectrometry, Fluorescence,
pubmed-meshheading:6488152-Spectrophotometry
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pubmed:year |
1984
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pubmed:articleTitle |
Binding of benzo(a)pyrene with peroxidase and its oxidation by peroxidase-H2O2 intermediate.
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pubmed:publicationType |
Journal Article
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