Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1988-2-29
pubmed:abstractText
The activities of guinea pig lung mitochondrial and microsomal glycerophosphate acyltransferase differed in sensitivity to polymyxin B1. At an antibiotic concentration of 1 mg/ml, the mitochondrial enzyme activity was stimulated twofold, but the microsomal enzyme activity was completely inhibited. Furthermore, the mitochondrial enzyme activity was stimulated by polymyxin B1 without the addition of exogenous acyl-CoA. Additional experiments ruled out the possibility of polymyxin B1 acting as a substrate for the mitochondrial acyltransferase. These results suggest either that the polymyxin B1 sensitivity of mitochondrial and microsomal glycerophosphate acyltransferase is different or that their accessibility to substrates is different because the two isoenzymes are located differently in the different phospholipid microenvironment of the membranes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0024-4201
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
757-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The differential effect of polymyxin B1 on guinea pig lung mitochondrial and microsomal glycerophosphate acyltransferase.
pubmed:affiliation
Department of Biochemistry, Meharry Medical College, Nashville, TN 37208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.