Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-11-23
pubmed:abstractText
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of detergent solubilized cytochrome P-450 fractions from normal and diabetic female rat liver microsomes revealed the induction of a 52,000 molecular weight microsomal hemeprotein in diabetic liver. Two major P-450 hemeproteins (DB IIA and DB IIB) were subsequently isolated from solubilized diabetic female rat hepatic P-450 fractions, while normal rat liver yielded only one major microsomal P-450, N IIA. When examined in a reconstituted drug metabolizing system, the aniline hydroxylation rate catalyzed by DB IIB (52,000 molecular weight) was 157% and 78% greater than the rates catalyzed by N IIA and DB IIA, respectively. The rates of ethylmorphine metabolism catalyzed by N IIA and DB IIB were similar; however, the rate of ethylmorphine metabolism catalyzed by DB IIA (54,000 molecular weight) was approximately 42% greater than the rates catalyzed by either N IIA or DB IIB. These results are compared to those previously obtained with P-450s isolated from diabetic male rat liver and indicate that diabetes induces P-450s with specific catalytic activities which can account for both the sex-dependent and sex-independent alterations in drug metabolism observed in diabetic rat liver.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0034-5164
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-90
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Catalytic activities of cytochrome P-450 from female rat liver: correlation with sex differences in drug metabolism in diabetic liver.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.