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Kinetics and thermodynamics of ouabain binding by intact turkey erythrocytes: effects of external sodium ion, potassium ion, and temperature
The kinetics of association and dissociation for the ouabain-Na+,K+- dependent ATPase complex have been studied in intact turkey erythrocytes as a function of external Na+ concentration, K+ concentration, and temperature. At free ligand concentrations substantially exceeding the concentration of ava...
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| Format: | Artigo |
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| Langue: | Inglês |
| Publié: |
The Rockefeller University Press
1980
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2228615/ https://ncbi.nlm.nih.gov/pubmed/6255063 |
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