ISSN:
1432-1041
Keywords:
Warfarin
;
Phenprocoumon
;
human serum albumin
;
non-esterified fatty acids
;
anticoagulant therapy
;
surgery
;
protein binding
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Medicine
Notes:
Summary The binding equilibria of warfarin and phenprocoumon with defatted human serum albumin were studied by equilibrium dialysis in 33 mM sodium phosphate buffer, pH 7.4, 37°C. The binding isotherms for both ligands were consistent with binding to two similar and independent sites in the albumin molecule. The binding affinity of warfarin was markedly increased on adding palmitic acid up to palmitate 4 mol per mol albumin and then it decreased. The binding affinity of phenprocoumon varied similarly but to a lesser degree. Serum samples were obtained from 14 patients under-going knee joint surgery, six consecutive samples from each patient. The binding affinity of warfarin and phenprocoumon added in low concentrations to the serum samples was consistently less than to purified albumin. The binding affinity for warfarin increased slightly with increasing fatty acid concentrations during surgery, but the increase was much less than expected from the in vitro studies. The binding of phenprocoumon in the serum samples was not influenced by changing fatty acid concentration. The binding affinity for both drugs decreased markedly during the three days following surgery.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00315474
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