Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-9-25
pubmed:abstractText
The alteration of two erythrocyte plasma membrane functions, acetylcholine hydrolysis and glucose exchange, by a series of structurally related small lipophilic compounds which exhibit antihemolytic behavior was studied. 2-Methyldimethylaminoazobenzene is a more potent inhibitor of acetylcholinesterase than the 3'-methyl analogue, while the unsubstituted compound fails to inhibit. Esterase inhibition by the 2-methyl compound is non-competitive and dependent on the anion composition of the assay buffer. The temperature dependence of acetylcholinesterase activity in the presence of the 2-methyl compound suggests that interaction with inhibitor is influenced by the state of lipids tightly bound to the enzyme. Glucose exchange is inhibited to the same extent by both methyl derivatives but not by the unsubstituted dye, and the temperature dependence in the presence of inhibitor is not grossly altered. The lack of correlation between inhibition of membrane function adn stabilization of erythrocytes against osmotic hemolysis is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
553
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
96-106
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Differential perturbation of erythrocyte membrane-associated transport and enzyme activities by structurally related lipophilic compounds.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.