ALTERATION OF THE ACETYLATION OF SULFONAMIDES BY PROTEIN BINDING, SULFINPYRAZONE, AND SURAMIN

Abstract

The following observations resulted from the studies: (1) bovine albumin interfered with the acetylation of sulfamethoxypyridazine. Apparently this was due to the binding of the sulfonamide to the protein since a similar effect was not observed with bovine globulin to which this sulfonamide was not bound. Furthermore, neither protein affected the acetylation of sulfanilamide whose binding to albumin was much less than that of sulfamethoxypyridazine; (2) in the presence of albumin, but not globulin, 2–25 times more of sulfinpyrazone and suramin, respectively, was required to inhibit the acetylation of sulfanilamide to the same extent as in the absence of the protein; (3) there appeared to be no consistent correlation among a number of sulfonamides between their binding to protein, "lipid solubility," pKa, and acetylation.