Protein Binding of Propisomide

This paper describes the protein binding of propisomide to human serum and isolated proteins using equilibrium dialysis. The drug is exclusively bound to α1-acid glycoprotein with high affinity. The binding is saturable even at low concentrations of the drug. Thus, the fraction unbound varied from 0...

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Bibliographic Details
Published in:Journal of pharmaceutical sciences 1985-05, Vol.74 (5), p.530-533
Main Authors: Zini, R., Barre, J., Defer, G., Jeanniot, J.P., Houin, G., Tillement, J.P.
Format: Article
Language:English
Subjects:
Adult
Anti-Arrhythmia Agents - blood
Binding, Competitive
Biological and medical sciences
Biotransformation
Blood Proteins - metabolism
Dialysis
Female
General pharmacology
Humans
Male
Medical sciences
Middle Aged
Orosomucoid - metabolism
Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions
Pharmacology. Drug treatments
Propylamines - blood
Protein Binding
Pyridines
Ultrafiltration
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Summary:This paper describes the protein binding of propisomide to human serum and isolated proteins using equilibrium dialysis. The drug is exclusively bound to α1-acid glycoprotein with high affinity. The binding is saturable even at low concentrations of the drug. Thus, the fraction unbound varied from 0.05 to 0.60 with decreasing serum concentration. The major metabolite of the drug or other drugs with affinity for α1-acid glycoprotein can displace propisomide from its binding site only when present in serum at high levels. Two ultrafiltration techniques are compared to equilibrium dialysis for the determination of serum protein binding of propisomide. Ultrafiltration does not give reliable results. Equilibrium dialysis is retained as an accurate method for the determination of the fraction unbound of propisomide.
ISSN:0022-3549
1520-6017
DOI:10.1002/jps.2600740507