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The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes

Ouabain binding by the human erythrocyte membrane is reversible, exhibits a high degree of chemical specificity, and can be detected at ouabain concentrations as low as 1 x 10(-10) M. The relation between ouabain binding and ouabain concentration can be described by a rectangular hyperbola permittin...

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Detalles Bibliográficos
Autores principales: Gardner, Jerry D., Conlon, Thomas P.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1972
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2226090/
https://www.ncbi.nlm.nih.gov/pubmed/4644328
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author Gardner, Jerry D.
Conlon, Thomas P.
author_facet Gardner, Jerry D.
Conlon, Thomas P.
author_sort Gardner, Jerry D.
collection PubMed
description Ouabain binding by the human erythrocyte membrane is reversible, exhibits a high degree of chemical specificity, and can be detected at ouabain concentrations as low as 1 x 10(-10) M. The relation between ouabain binding and ouabain concentration can be described by a rectangular hyperbola permitting determination of the maximal binding (B (max)) and the ouabain concentration at which ouabain binding is half-maximal (K(B)). Reducing the external sodium concentration increased K(B), while reducing the external potassium concentration decreased K(B). Neither cation altered B (max) The reciprocal of K(B) was a linear function of the sodium concentration at sodium concentrations ranging from 0 to 150 mM. Conversely, the relation between the reciprocal of K(B) and the external potassium concentration was nonlinear, and raising the potassium concentration above 4 mM produced no further increase in K(B). These results are compatible with a model which postulates that the erythrocyte membrane contains a finite number of receptors each composed of a glycoside-binding site and a cation-binding site. When sodium occupies the cation-binding site, the affinity of the glycoside site for ouabain is increased; when potassium occupies the cation-binding site the affinity of the glycoside site for ouabain is decreased.
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spelling pubmed-22260902008-04-23 The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes Gardner, Jerry D. Conlon, Thomas P. J Gen Physiol Article Ouabain binding by the human erythrocyte membrane is reversible, exhibits a high degree of chemical specificity, and can be detected at ouabain concentrations as low as 1 x 10(-10) M. The relation between ouabain binding and ouabain concentration can be described by a rectangular hyperbola permitting determination of the maximal binding (B (max)) and the ouabain concentration at which ouabain binding is half-maximal (K(B)). Reducing the external sodium concentration increased K(B), while reducing the external potassium concentration decreased K(B). Neither cation altered B (max) The reciprocal of K(B) was a linear function of the sodium concentration at sodium concentrations ranging from 0 to 150 mM. Conversely, the relation between the reciprocal of K(B) and the external potassium concentration was nonlinear, and raising the potassium concentration above 4 mM produced no further increase in K(B). These results are compatible with a model which postulates that the erythrocyte membrane contains a finite number of receptors each composed of a glycoside-binding site and a cation-binding site. When sodium occupies the cation-binding site, the affinity of the glycoside site for ouabain is increased; when potassium occupies the cation-binding site the affinity of the glycoside site for ouabain is decreased. The Rockefeller University Press 1972-11-01 /pmc/articles/PMC2226090/ /pubmed/4644328 Text en Copyright © 1972 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Gardner, Jerry D.
Conlon, Thomas P.
The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title_full The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title_fullStr The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title_full_unstemmed The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title_short The Effects of Sodium and Potassium on Ouabain Binding by Human Erythrocytes
title_sort effects of sodium and potassium on ouabain binding by human erythrocytes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2226090/
https://www.ncbi.nlm.nih.gov/pubmed/4644328
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