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Title: Consequences of the N-B transition of albumin for the binding of warfarin in human serum. Author: van der Giesen WF, Wilting J. Journal: Biochem Pharmacol; 1983 Jan 15; 32(2):281-5. PubMed ID: 6870956. Abstract: The protein binding of warfarin in serum has been studied by means of circular dichroism and equilibrium dialysis. Evidence was found that the N-B transition of albumin, occurring around physiological pH, takes place not only in solutions of pure albumin but also in serum. The protein binding of warfarin in serum is pH-dependent and increases with pH especially around physiological pH. This pH-dependent serum binding of warfarin can be reasonably explained by the N-B transition of albumin. The effect of Ca2+ and Mg2+ on the protein binding of warfarin in serum is negligible at pH 7.4, whereas at this pH Cl- increases the free-warfarin concentration by a competitive displacement.[Abstract] [Full Text] [Related] [New Search]