Matches in SemOpenAlex for { <https://semopenalex.org/work/W2047806243> ?p ?o ?g. }
Showing items 1 to 92 of
92
with 100 items per page.
- W2047806243 endingPage "487" @default.
- W2047806243 startingPage "480" @default.
- W2047806243 abstract "The nonlinear temperature-activity relationship of membrane preparations of (Na+ + K+)-ATPase gives rise to discontinuities in Arrhenius plots of this enzyme. The different apparent energies of activation of (Na+ + K+) — ATPase which are observed above and below the critical temperature of the system have been considered to result from different conformational forms of the enzyme protein. Because both activation of (Na+ + K+)-ATPase by cations, and its specific inhibition by cardiac glycosides may be influenced by the conformational form of the enzyme protein, we have reexamined the effect of temperature upon the activation energy of the system under the different experimental conditions of cation activation and ouabain inhibition. Our results indicate that the activation of (Na+ + K+)-ATPase by cations, is less influenced by change in temperature than is inhibition of the enzyme by ouabain. In addition, mild lipolysis by phospholipase-A had a marked effect upon the ouabain-dependent response of the enzyme to temperature, but not upon the cation-dependent response. The effect of phospholipase-A can be overcome by reincubation of the treated preparation with phosphatidyl serine. We conclude that the ouabain-dependent temperature effects of (Na+ + K+)-ATPase are more dependent upon the integrity and nature of the membrane lipids than are the cation-dependent responses. It is possible that phosphatidyl serine plays a unique role in this regard." @default.
- W2047806243 created "2016-06-24" @default.
- W2047806243 creator A5019014799 @default.
- W2047806243 creator A5068886357 @default.
- W2047806243 creator A5081560014 @default.
- W2047806243 date "1975-04-01" @default.
- W2047806243 modified "2023-09-26" @default.
- W2047806243 title "Temperature-activity relationships of cation activation and ouabain inhibition of (Na+ + K+)-ATPase" @default.
- W2047806243 cites W1550104893 @default.
- W2047806243 cites W1971455512 @default.
- W2047806243 cites W1975301251 @default.
- W2047806243 cites W1975354192 @default.
- W2047806243 cites W1985979935 @default.
- W2047806243 cites W1995954631 @default.
- W2047806243 cites W2004205850 @default.
- W2047806243 cites W2020855710 @default.
- W2047806243 cites W2023764880 @default.
- W2047806243 cites W2023905787 @default.
- W2047806243 cites W2025041851 @default.
- W2047806243 cites W2025150943 @default.
- W2047806243 cites W2030960955 @default.
- W2047806243 cites W2039046168 @default.
- W2047806243 cites W2044045196 @default.
- W2047806243 cites W2050569975 @default.
- W2047806243 cites W2056399277 @default.
- W2047806243 cites W2065906995 @default.
- W2047806243 cites W2081456823 @default.
- W2047806243 cites W2082631570 @default.
- W2047806243 cites W2091791025 @default.
- W2047806243 cites W2315141432 @default.
- W2047806243 cites W2400398545 @default.
- W2047806243 cites W2400921612 @default.
- W2047806243 doi "https://doi.org/10.1016/0003-9861(75)90490-7" @default.
- W2047806243 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/123731" @default.
- W2047806243 hasPublicationYear "1975" @default.
- W2047806243 type Work @default.
- W2047806243 sameAs 2047806243 @default.
- W2047806243 citedByCount "32" @default.
- W2047806243 crossrefType "journal-article" @default.
- W2047806243 hasAuthorship W2047806243A5019014799 @default.
- W2047806243 hasAuthorship W2047806243A5068886357 @default.
- W2047806243 hasAuthorship W2047806243A5081560014 @default.
- W2047806243 hasConcept C125209161 @default.
- W2047806243 hasConcept C12554922 @default.
- W2047806243 hasConcept C12927208 @default.
- W2047806243 hasConcept C178790620 @default.
- W2047806243 hasConcept C181199279 @default.
- W2047806243 hasConcept C185592680 @default.
- W2047806243 hasConcept C23265538 @default.
- W2047806243 hasConcept C2777339483 @default.
- W2047806243 hasConcept C2779133857 @default.
- W2047806243 hasConcept C537181965 @default.
- W2047806243 hasConcept C55493867 @default.
- W2047806243 hasConcept C86183883 @default.
- W2047806243 hasConcept C86803240 @default.
- W2047806243 hasConcept C95121573 @default.
- W2047806243 hasConceptScore W2047806243C125209161 @default.
- W2047806243 hasConceptScore W2047806243C12554922 @default.
- W2047806243 hasConceptScore W2047806243C12927208 @default.
- W2047806243 hasConceptScore W2047806243C178790620 @default.
- W2047806243 hasConceptScore W2047806243C181199279 @default.
- W2047806243 hasConceptScore W2047806243C185592680 @default.
- W2047806243 hasConceptScore W2047806243C23265538 @default.
- W2047806243 hasConceptScore W2047806243C2777339483 @default.
- W2047806243 hasConceptScore W2047806243C2779133857 @default.
- W2047806243 hasConceptScore W2047806243C537181965 @default.
- W2047806243 hasConceptScore W2047806243C55493867 @default.
- W2047806243 hasConceptScore W2047806243C86183883 @default.
- W2047806243 hasConceptScore W2047806243C86803240 @default.
- W2047806243 hasConceptScore W2047806243C95121573 @default.
- W2047806243 hasIssue "2" @default.
- W2047806243 hasLocation W20478062431 @default.
- W2047806243 hasLocation W20478062432 @default.
- W2047806243 hasOpenAccess W2047806243 @default.
- W2047806243 hasPrimaryLocation W20478062431 @default.
- W2047806243 hasRelatedWork W1155355392 @default.
- W2047806243 hasRelatedWork W1994162629 @default.
- W2047806243 hasRelatedWork W2039011601 @default.
- W2047806243 hasRelatedWork W2047670402 @default.
- W2047806243 hasRelatedWork W2047806243 @default.
- W2047806243 hasRelatedWork W2081107494 @default.
- W2047806243 hasRelatedWork W2087236557 @default.
- W2047806243 hasRelatedWork W2407846868 @default.
- W2047806243 hasRelatedWork W2473494848 @default.
- W2047806243 hasRelatedWork W4230397874 @default.
- W2047806243 hasVolume "167" @default.
- W2047806243 isParatext "false" @default.
- W2047806243 isRetracted "false" @default.
- W2047806243 magId "2047806243" @default.
- W2047806243 workType "article" @default.