Linked Life Data

9920283

Source:http://linkedlifedata.com/resource/pubmed/id/9920283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-2-11
pubmed:abstractText
Membrane-bound (Ca2+ + Mg2+)-ATPase activity from human erythrocyte white ghosts in the calmodulin-activated state was inhibited by DMSO in concentrations of 3% (v/v) and above. At 10%, DMSO inhibited calmodulin activation by 47.7%, while basal, calmodulin-independent (Ca2+ + Mg2+)-ATPase and (Mg2+)-ATPase activity remained unaffected. (Na+ + K+)-ATPase activity was also reduced but exhibited a greater IC50. Concentration-effect analyses showed the inhibition by 10% DMSO to be a reversible, non-competitive effect with regard to calmodulin, Ca2+, and substrate activation. Calmodulin-stimulated processes may be more susceptible to inhibition by DMSO than related enzymatic catalysis, and thus may help explain the multitude of reported cellular events caused by the solvent. Furthermore, DMSO affected membrane-associated enzymatic mechanisms opposite to those reported for purified enzyme outside its native membrane environment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-44
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Inhibition of calmodulin-stimulated (Ca2+ + Mg2+)-ATPase activity by dimethyl sulfoxide.
pubmed:affiliation
Department of Pharmacology and Toxicology, Indiana University School of Medicine, Evansville 47712, USA.
pubmed:publicationType
Journal Article