The characteristics of the binding of 12-alpha-[3H]-digoxin to the membranes of intact human erythrocytes: relevance to digoxin therapy.
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.
D002301:Cardiac Glycosides / Q000494:pharmacology; D004077:Digoxin / Q000097:blood* / Q000627:therapeutic use; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D013696:Temperature; D013997:Time Factors
D002301:Cardiac Glycosides; D010042:Ouabain; D004077:Digoxin; D011188:Potassium