Quabain: Temporal relationship between the inotropic effect and the in vitro binding to, and dissociation from, (Na++K+)-activated ATPase-Reference-Cited by-同舟云学术

Quabain: Temporal relationship between the inotropic effect and the in vitro binding to, and dissociation from, (Na++K+)-activated ATPase

Published:1973 Issue:2 Volume:277 Page:151-162
ISSN:0028-1298
Container-title:Naunyn-Schmiedeberg's Archives of Pharmacology
language:en
Short-container-title:Naunyn-Schmiedeberg's Arch. Pharmacol.

Author:

Akera T.,Baskin S. I.,Tobin T.,Brody T. M.

Publisher

Springer Science and Business Media LLC

Subject

Pharmacology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/BF00501156.pdf

Reference35 articles.

1. Akera, T.: Quantitative aspects of the interaction between ouabain and (Na++K+)-activated ATPase in vitro. Biochim. biophys. Acta (Amst.) 249, 53?62 (1971).

2. 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).

3. Akera, T., Larsen, F. S., Brody, T. M.: The effect of ouabain on sodium- and potassium-activated adenosine triphosphatase from the hearts of several mammalian species. J. Pharmacol. exp. Ther. 170, 17?26 (1969).

4. Akera, T., Larsen, F. S., Brody, T. M.: Correlation of cardiac sodium- and potassium-activated adenosine triphosphatase activity with ouabain-induced inotropic stimulation. J. Pharmacol. exp. Ther. 173, 145?151 (1970).

5. Allen, J. C., Besch, H. R., Glick, G., Schwartz, A.: The binding of tritiated ouabain to sodium- and potassium-activated adenosine triphosphatase and cardiac relaxing system of perfused dog heart. Molec. Pharmacol. 6, 441?443 (1970a).

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