FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1966944725> ?p ?o ?g. }

• W1966944725 endingPage "346" @default.
• W1966944725 startingPage "335" @default.
• W1966944725 abstract "This paper reports on the kinetic and thermodynamic parameters describing the interaction of selected digitalis derivatives with hog and guinea-pig cardiac (Na+ + K+)-ATPase (Na+/K+-transporting ATPase EC 3.6.1.37). 32 digitalis derivatives were characterized as to the values of the ΔG°′, ΔG≠, and ΔG≠ quantities in their interaction with (Na+ + K+)-ATPase from hog cardiac muscle in the presence of ATP, Mg2+, Na+ and K+. Nine derivatives were additionally characterized as to the values of the ΔH°′, ΔS°′, ΔH≠, ΔS≠, ΔH≠, ΔS≠, and ΔS≠ quantities in their interaction with the hog enzyme promoted by ATP, Mg2+ and Na+ in the presence or absence of K+. The formation of the inhibitory complexes is in any case an endothermic, entropically driven process. The Gibbs energy barriers in the formation and dissociation of the complexes, ΔG≠ and ΔG≠, are imposed by large, unfavourable ΔH≠ values. K+ decreases the ΔG°′ value by increasing the ΔG≠ value more than the ΔG≠ value. In comparison with hog (Na+ + K+)-ATPase, the interaction of three derivatives with guinea-pig cardiac enzyme in the presence of ATP, Mg2+, Na+ and K+ is characterized by lower ΔG°′ values caused by lower favourable ΔS°′ values, and is accompanied by lower ΔG≠ values. The magnitude of the kinetic parameters and the characteristic of the thermodynamic quantities describing the interaction between various digitalis derivatives and (Na+ + K+)-ATPase, indicate the induction of substantial conformational changes in the enzyme protein. A large entropy gain in the enzyme protein, observed irrespective of enzyme origin and ligation, appears to be the common denominator of the inhibitory action of all digitalis derivatives studied, suggesting that the digitalis-elicited relaxation of high conformational energy (negentropy strain) of the enzyme protein is the thermodynamic essence of the reversible inactivation of (Na+ + K+)-ATPase." @default.
• W1966944725 created "2016-06-24" @default.
• W1966944725 creator A5002565998 @default.
• W1966944725 creator A5003024714 @default.
• W1966944725 creator A5020983655 @default.
• W1966944725 creator A5033632935 @default.
• W1966944725 creator A5039532182 @default.
• W1966944725 creator A5047559745 @default.
• W1966944725 creator A5069148881 @default.
• W1966944725 date "1988-01-01" @default.
• W1966944725 modified "2023-10-14" @default.
• W1966944725 title "The thermodynamic essence of the reversible inactivation of Na+/K+-transporting ATPase by various digitalis derivatives is relaxation of enzyme conformational energy" @default.
• W1966944725 cites W1508147765 @default.
• W1966944725 cites W1523387290 @default.
• W1966944725 cites W1564076413 @default.
• W1966944725 cites W1590045255 @default.
• W1966944725 cites W1775749144 @default.
• W1966944725 cites W1975328649 @default.
• W1966944725 cites W1992979672 @default.
• W1966944725 cites W1993836052 @default.
• W1966944725 cites W1999568444 @default.
• W1966944725 cites W2012981999 @default.
• W1966944725 cites W2020629542 @default.
• W1966944725 cites W2028227377 @default.
• W1966944725 cites W2035257912 @default.
• W1966944725 cites W2039427220 @default.
• W1966944725 cites W2047363704 @default.
• W1966944725 cites W2051991390 @default.
• W1966944725 cites W2059348176 @default.
• W1966944725 cites W2059737570 @default.
• W1966944725 cites W2075292333 @default.
• W1966944725 cites W2079237812 @default.
• W1966944725 cites W2085722214 @default.
• W1966944725 cites W2093713534 @default.
• W1966944725 cites W2125816807 @default.
• W1966944725 cites W2166244817 @default.
• W1966944725 cites W2171295293 @default.
• W1966944725 cites W230984257 @default.
• W1966944725 cites W4253232718 @default.
• W1966944725 cites W66493300 @default.
• W1966944725 doi "https://doi.org/10.1016/0005-2736(88)90256-8" @default.
• W1966944725 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2827773" @default.
• W1966944725 hasPublicationYear "1988" @default.
• W1966944725 type Work @default.
• W1966944725 sameAs 1966944725 @default.
• W1966944725 citedByCount "15" @default.
• W1966944725 countsByYear W19669447252016 @default.
• W1966944725 crossrefType "journal-article" @default.
• W1966944725 hasAuthorship W1966944725A5002565998 @default.
• W1966944725 hasAuthorship W1966944725A5003024714 @default.
• W1966944725 hasAuthorship W1966944725A5020983655 @default.
• W1966944725 hasAuthorship W1966944725A5033632935 @default.
• W1966944725 hasAuthorship W1966944725A5039532182 @default.
• W1966944725 hasAuthorship W1966944725A5047559745 @default.
• W1966944725 hasAuthorship W1966944725A5069148881 @default.
• W1966944725 hasConcept C106301342 @default.
• W1966944725 hasConcept C121332964 @default.
• W1966944725 hasConcept C126322002 @default.
• W1966944725 hasConcept C135889238 @default.
• W1966944725 hasConcept C146477669 @default.
• W1966944725 hasConcept C147789679 @default.
• W1966944725 hasConcept C150394285 @default.
• W1966944725 hasConcept C178790620 @default.
• W1966944725 hasConcept C181199279 @default.
• W1966944725 hasConcept C185592680 @default.
• W1966944725 hasConcept C20976626 @default.
• W1966944725 hasConcept C23265538 @default.
• W1966944725 hasConcept C2776445394 @default.
• W1966944725 hasConcept C2778198053 @default.
• W1966944725 hasConcept C32909587 @default.
• W1966944725 hasConcept C55493867 @default.
• W1966944725 hasConcept C62520636 @default.
• W1966944725 hasConcept C69308434 @default.
• W1966944725 hasConcept C71240020 @default.
• W1966944725 hasConcept C71924100 @default.
• W1966944725 hasConcept C8010536 @default.
• W1966944725 hasConcept C97355855 @default.
• W1966944725 hasConceptScore W1966944725C106301342 @default.
• W1966944725 hasConceptScore W1966944725C121332964 @default.
• W1966944725 hasConceptScore W1966944725C126322002 @default.
• W1966944725 hasConceptScore W1966944725C135889238 @default.
• W1966944725 hasConceptScore W1966944725C146477669 @default.
• W1966944725 hasConceptScore W1966944725C147789679 @default.
• W1966944725 hasConceptScore W1966944725C150394285 @default.
• W1966944725 hasConceptScore W1966944725C178790620 @default.
• W1966944725 hasConceptScore W1966944725C181199279 @default.
• W1966944725 hasConceptScore W1966944725C185592680 @default.
• W1966944725 hasConceptScore W1966944725C20976626 @default.
• W1966944725 hasConceptScore W1966944725C23265538 @default.
• W1966944725 hasConceptScore W1966944725C2776445394 @default.
• W1966944725 hasConceptScore W1966944725C2778198053 @default.
• W1966944725 hasConceptScore W1966944725C32909587 @default.
• W1966944725 hasConceptScore W1966944725C55493867 @default.
• W1966944725 hasConceptScore W1966944725C62520636 @default.
• W1966944725 hasConceptScore W1966944725C69308434 @default.
• W1966944725 hasConceptScore W1966944725C71240020 @default.
• W1966944725 hasConceptScore W1966944725C71924100 @default.
• W1966944725 hasConceptScore W1966944725C8010536 @default.

• next