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British Journal of Clinical Pharmacology logoLink to British Journal of Clinical Pharmacology
. 1979 Aug;8(2):115–124. doi: 10.1111/j.1365-2125.1979.tb05809.x

The characteristics of the binding of 12-alpha-[3H]-digoxin to the membranes of intact human erythrocytes: relevance to digoxin therapy.

A R Ford, J K Aronson, D G Grahame-Smith, J A Rose
PMCID: PMC1429769  PMID: 486288

Abstract

1 The characteristics of the binding of 12-alpha-[3H]-digoxin to the membranes of intact human erythrocytes are described. 2 Only one class of binding site can be demonstrated. Binding is time- and temperature-dependent, saturable and slowly reversible; it is inhibited by other cardiac glycosides and by potassium. 3 Pre-incubation with unlabelled digoxin reduces the subsequent binding of 12-alpha-[3H]-digoxin in stoichiometric fashion. 4 The possible application of the measurement of the binding of 12-alpha-[3H]-digoxin to the study of biochemical pharmacological events occurring during digoxin therapy is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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