Reduction of the equilibrium binding of cardiac glycosides and related compounds to Na+, K+-ATPase as a possible mechanism for the potassium-induced reversal of their toxicity

Author:

Akera Tai,Temma Kyosuke,Wiest Sally A.,Brody Theodore M.

Publisher

Springer Science and Business Media LLC

Subject

Pharmacology,General Medicine

Reference39 articles.

1. Akera, T.: Quantitative aspects of the interaction between ouabain and the Na+, K+-ATPase. Biochim. Biophys. Acta. 245, 53?62 (1971)

2. Akera, T., Baskin, S.I., Tobin, T., Brody, T.M.: Ouabain: Temporal relationship between the inotropic effect and the in vitro binding to, and dissociation from, (Na+, K+)-activated ATPase. Naunyn-Schmiedeberg's Arch. Pharmacol. 277, 151?162 (1973)

3. Akera, T., Brody, T. M.: Membrane adenosine triphosphatase: The effect of potassium on the formation and dissociation of the ouabain-enzyme complex. J. Pharmacol. Exp. Ther. 176, 545?557 (1971)

4. Akera, T., Ku, D., Tobin, T., Brody, T. M.: The complexes of ouabain with sodium-and potassium-activated adenosine triphosphatase formed with various ligands: Relationship to the complex formed in the beating heart. Mol. Pharmacol. 12, 101?114 (1976)

5. Akera, T., Tobin, T., Gatti, A., Shieh, I.-S., Brody, T. M.: Effect of potassium on the conformational state of the complex of ouabain with sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 10, 509?518 (1974)

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