Effect of salicylate on the binding of sulfonamides to bovine serum albumin.

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Abstract
Displacement of 8 sulfonamides by sodium salicylate [a non-steroidal antiinflammatory agent] from the binding sites of bovine serum albumin (BSA) was studied by the equilibrium dialysis method at pH 7.4 and 37.degree.. Amount of sulfonamides displaced by the addition of salicylate (1 or 3 mM) were linearly correlated with their amount bound to the binding sites of BSA in the absence of salicylate. Double-reciprocal plots of the binding of sulfamethoxazole to BSA with and without salicylate, following Langmuir''s isotherms, resulted in linear curves with a common ordinate intercept. Apparently, the inhibitory effects of salicylate on the binding of sulfamethoxazole to albumin were competitively performed at the same binding site on the protein.