Effect of chloride ions on the interaction between salicylic acid and human serum albumin studied by frontal affinity chromatography.

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Abstract
The interaction of salicylic acid with human serum albumin (HSA) was studied at 4.degree. C by a frontal affinity chromatographic technique employing HSA monomer immobilized on agarose beads in 2 buffer systems, i.e., Tris-HCl and phosphate buffers. A large difference in the apparent binding constants in these buffer systems was almost entirely attributed to the presence of Cl- in Tris-HCl buffers. The inhibitory effect of Cl- was directly demonstrated to be due to the binding of Cl- to HSA, and other components of the buffers had little effect. The data can be interpreted on the basis of competitive binding at sites other than the primary Cl- binding sites.

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