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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-12-20
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0305-7232
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-29
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Binding of benzo(a)pyrene with peroxidase and its oxidation by peroxidase-H2O2 intermediate.
pubmed:publicationType
Journal Article