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

Journal article

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.

Authors: Ford, A; Aronson, J; Grahame-Smith, D; Rose, J

• Publication status: Published
• Journal: British journal of clinical pharmacology
• Volume: 8
• Issue: 2
• Pages: 115-124
• Publication date: 1979-08-01
• DOI: 10.1111/j.1365-2125.1979.tb05809.x
• EISSN: 1365-2125
• ISSN: 0306-5251
• Language: English
• Keywords: Kinetics; Potassium; Time Factors; Erythrocytes; Erythrocyte Membrane; Cardiac Glycosides; Digoxin; Temperature; Humans; Ouabain