Abstract
The protein binding of warfarin in serum has been studied by means of circular dichroism and equilibrium dialysis. Evidence was found that the NB 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 NB transition of albumin. The effect of Ca 2+ and Mg 2+ 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
