Phenytoin binding to human albumin.
Binding of phenytoin to human plasma proteins and to human serum albumin is studied using equilibrium dialysis method at pH 7.4 and 37 degrees C. Phenytoin is mainly bound to albumin, the percentage of bound drug being constant over a wide range of total drug concentrations. Calculation of the drug binding parameters show a low affinity, k = 745 M-1, and a high number of binding sites, n = 8. Palmitic acid and some acidic drugs, warfarin and phenylbutazone added to human serum albumin, decreased phenytoin binding in a non competitive way. Basic and non-ionizable drugs, on the other hand, did not modify phenytoin binding.
D000817:Anilino Naphthalenesulfonates / Q000097:blood; D005230:Fatty Acids, Nonesterified / Q000378:metabolism; D006801:Humans; D007099:Imipramine / Q000494:pharmacology; D010169:Palmitic Acids / Q000494:pharmacology; D010653:Phenylbutazone / Q000097:blood; D010672:Phenytoin / Q000097:blood*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D014859:Warfarin / Q000494:pharmacology
D000817:Anilino Naphthalenesulfonates; D005230:Fatty Acids, Nonesterified; D010169:Palmitic Acids; D012709:Serum Albumin; D014859:Warfarin; D010672:Phenytoin; D010653:Phenylbutazone; D007099:Imipramine