Linked Life Data

3495296

Source:http://linkedlifedata.com/resource/pubmed/id/3495296

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-7-15
pubmed:abstractText
The effects of exogenous phospholipase A2, oleic acid and lysolecithines on oxidative NADPH-dependent O-dealkylation of 7-ethoxycumarin in liver microsomes of phenobarbital- and 3-methylcholanthrene-induced and non-induced rats were studied. Oleic acid up to the concentration of 100 micrograms/mg of protein did not inhibit this process. gamma-Myristoyl and gamma-palmitoyl lysolecithines decreased the reaction rate already at concentrations of 2-4 micrograms/mg of protein. Oleic acid was attached to cytochrome P-450 according to type I binding, whereas lysolecithines did not bind to the cytochrome. Thus, in the presence of phospholipase A2 in liver microsomes of non-induced rats, when the phospholipid hydrolysis products are accumulated at low concentrations, 7-ethoxycumarin deethylase is inhibited by lysophospholipids but not by free fatty acids. In 3-methylcholanthrene-induced microsomes the sensitivity of O-deethylation of 7-ethoxycumarin to the inhibiting effect of phospholipase A2 or lysolecithine is lower than that in non-induced or phenobarbital-induced microsomes.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
459-68
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
[Inhibition of the dealkylating activity of cytochrome P-450 isoforms in rat liver microsomes by the products of phospholipase A2-induced phospholipid hydrolysis].
pubmed:publicationType
Journal Article, In Vitro, English Abstract