Linked Life Data

1726082

Source:http://linkedlifedata.com/resource/pubmed/id/1726082

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-6-23
pubmed:abstractText
A previously unidentified cytochrome P-450ap possessing the highest aminopyrine-N-demethylase activity has been isolated from liver microsomes of 4-isopropylaminoantipyrine-induced rats, using affinity chromatography in combination with ion-exchange chromatography with subsequent separation on a hydroxyapatite column. The isolated cytochrome P-450ap has the following characteristics: Mr = 49 kD, CO-peak maximum at 450.5 nm, rate of demethylation in a reconstituted system for aminopyrine of 25.5 nmoles of HCHO/min per nmole of P-450, and for benzphetamine a rate of 17.0 nmoles of HCHO/min per nmole of P-450. The hemoprotein synthesis is paralleled by the synthesis of a protein with Mr of 51 kD. Immunochemical analysis permitted the identification of the latter protein as cytochrome P-450b. It was, demonstrated that cytochrome P-450ap does not interact with the antibodies to the major phenobarbital induced form, i.e. with cytochrome P-450b.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0378-7966
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-7
pubmed:dateRevised
2011-2-2
pubmed:meshHeading
pubmed:articleTitle
Aminopyrine-N-demethylase. II. Characterization of a unique monooxygenase isoform P-450ap.
pubmed:affiliation
Laboratory of Xenobiochemistry, Academy of Medical Sciences, Siberian Division, Novosibirsk, USSR.
pubmed:publicationType
Journal Article