The effect of chloride on the binding of warfarin to albumin as a function of pH
| Autor: | Jaap Wilting, Lambert H.M. Janssen, Willem F. van der Giesen |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Circular dichroism
Protein Conformation Inorganic chemistry Serum albumin Plasma protein binding Biochemistry Chloride Chlorides medicine Humans Binding site Serum Albumin Pharmacology biology Chemistry Albumin Hydrogen-Ion Concentration Human serum albumin Binding constant Kinetics biology.protein Calcium Warfarin Dialysis medicine.drug Protein Binding |
| Zdroj: | Biochemical pharmacology. 30(10) |
| ISSN: | 0006-2952 |
| Popis: | The effect of chloride on the binding of warfarin to human serum albumin between pH 6 and 9.5 has been studied by circular dichroism and equilibrium dialysis. The molar ellipticity of the warfarin-albumin complex is hardly affected by chloride ions when the protein is in the B conformation, whereas in the N conformation this spectroscopic quantity is greatly reduced in the presence of chloride ions. At all pHs the affinity of warfarin for albumin is decreased by the chloride ion. At pH 7.4 this is primarily due to a displacement of warfarin from its high affinity site. The binding constant of chloride for this specific site is about 20 M −1 . At the other pHs investigated chloride affects also the N-B transition. However, the affinity of chloride for the warfarin binding site of albumin is hardly affected by the N-B transition. The physiological importance of the N-B transition in changing albumin binding parameters for drugs and endogeneous compounds caused by small changes in blood concentrations of hydrogen and other ions is discussed. |
| Databáze: | OpenAIRE |
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