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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-12-28
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pubmed:abstractText |
We have measured the potency of 17 digitalis derivatives on cardiac (Na+ + K+)-ATPase from the digitalis-sensitive species, beef, cat and human. The potencies are given as the dissociation constant (KD-value) calculated from the concentration of unlabelled compound which inhibited 3H-ouabain binding by 50%, or from Scatchard or Woolf analyses. KD-values calculated by these independent methods were similar. As previously noted, structure-activity relationship (SAR) studies show that the binding of the whole molecule is necessary for optimal potency. The 3H-labelled derivatives of five of these compounds were used to measure the association and dissociation rate constants with cardiac (Na+ + K+)-ATPase. The rate constants for cat and human cardiac (Na+ + K+)-ATPase were very similar. Further, KD-values on cat and human cardiac (Na+ + K+)-ATPase for the 17 compounds tested showed a close correlation (r greater than 0.99), indicating that the cat heart is a suitable model for digitalis effects on the human heart.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0301-4533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
229-40
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:6095779-Animals,
pubmed-meshheading:6095779-Binding Sites,
pubmed-meshheading:6095779-Cats,
pubmed-meshheading:6095779-Cattle,
pubmed-meshheading:6095779-Digitalis Glycosides,
pubmed-meshheading:6095779-Humans,
pubmed-meshheading:6095779-Kinetics,
pubmed-meshheading:6095779-Myocardium,
pubmed-meshheading:6095779-Ouabain,
pubmed-meshheading:6095779-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:6095779-Species Specificity,
pubmed-meshheading:6095779-Tritium
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pubmed:year |
1984
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pubmed:articleTitle |
Binding of digitalis derivatives to beef, cat and human cardiac (Na+ + K+)-ATPase. Affinity and kinetic constants.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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