Study of drug-protein binding by affinity chromatography: interaction of bovine serum albumin and salicylic acid.
The affinity chromatographic technique was used to study the interaction of bovine serum albumin and salicylic acid at 3.3 +/- 1.1 degrees. Beaded agarose gel, on which the albumin was immobilized by covalent linkage, was packed in a column as an affinity adsorbent. Frontal analysis was performed on this column to evaluate the binding parameters for the interaction. The effect of albumin immobilization on drug binding was investigated by comparing the binding parameters of two affinity adsorbents, directly coupled albumin and albumin coupled through a spacer arm. The latter mode of attachment gave binding characteristics comparable to those of the soluble albumin. The method is simple and precise. The affinity adsorbent can be used repeatedly for many months for various drugs, including those that do not diffuse through dialysis membranes.
D002846:Chromatography, Affinity; D004347:Drug Interactions; D011485:Protein Binding; D012459:Salicylates / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D012459:Salicylates; D012710:Serum Albumin, Bovine