| Literature DB >> 486288 |
A R Ford, J K Aronson, D G Grahame-Smith, J A Rose.
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.Entities:
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Year: 1979 PMID: 486288 PMCID: PMC1429769 DOI: 10.1111/j.1365-2125.1979.tb05809.x
Source DB: PubMed Journal: Br J Clin Pharmacol ISSN: 0306-5251 Impact factor: 4.335