Linked Life Data

8042409

Source:http://linkedlifedata.com/resource/pubmed/id/8042409

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-8-23
pubmed:abstractText
As a noncompetitive inhibitor of pig gastric H+/K(+)-ATPase, indomethacin inhibited the H+ transportation function of the enzyme, leading to not only the obvious dissipation of H+/K(+)-ATPase-generated H+ gradients, but also the decreasing of the H+ gradient formation ability of the enzyme. 4% of indomethacin was able to penetrate into the lipid bilayer of H+/K(+)-ATPase vesicles at 0.15 mg/ml protein concentration, which showed an influence of indomethacin to the membrane. Indomethacin reduced the membrane fluidity of H+/K(+)-ATPase vesicles significantly. It also damaged the conformation of membrane protein extraordinarily, which was evidenced by decreasing the intrinsic fluorescence of H+/K(+)-ATPase. From the results, we suggest that the effect of indomethacin on H+/K(+)-ATPase is taken place by its inhibition on H+/K(+)-ATPase protein, as well as by its influence on the membrane lipid bilayer of H+/K(+)-ATPase vesicles.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0001-5334
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
[Effect of indomethacin on H+ transportation of pig gastric H+/K(+)-ATPase].
pubmed:affiliation
Division of Biomembrane, Chinese Academy of Science, Beijing.
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't