Linked Life Data

3682416

Source:http://linkedlifedata.com/resource/pubmed/id/3682416

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-1-12
pubmed:abstractText
Drug oxidations by horseradish peroxidase (HRP), myoglobin (Mb) and cytochrome P-450cam (P-450cam) reconstituted with synthetic hemes were studied in comparison with a form of cytochrome P-450 purified from liver microsomes of polychlorinated biphenyl (PCB)-treated rats. N,N-Dimethylaniline (DMA) and 7-isopropoxycoumarin were hardly dealkylated by the heme-substituted proteins in the presence of NADPH-cytochrome c (P-450) reductase and NADPH, while substantial activity of this kind was observed in the presence of hydrogen peroxide or cumene hydroperoxide as oxygen donors. Specific activity varied, depending on the substrates, oxygen donors, heme derivatives and apoproteins employed. Very high levels of activity were observed in hydrogen peroxide-dependent DMA N-demethylation with HRP substituted with certain hemes. The highest level of activity was about two hundred times as high as that of rat liver cytochrome P-450. The relationship between such activity and the chemical structure of heme derivatives was discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-5198
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Drug oxidation activities of horseradish peroxidase, myoglobin and cytochrome P-450cam reconstituted with synthetic hemes.
pubmed:affiliation
Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't