Abstract
The protein binding of indomethacin, sulindak and diclofenac sodium is studied in the presence of some competitors: phenylbutazon and diazepam. A high-performance liquid affinity chromatography based on chiral stationary phases with immobilized human serum albumin is used. The competition of the markers and the drugs for two major high- and low-affinity binding sites is investigated. Using a mathematical procedure proposed by the same authors in a previous work the affinity constants of the binding drugs and markers for both types of site are calculated. An analogous behaviour is established for the three drugs—they have nearly the same affinity for the primary binding sites marked by phenylbutazon and diazepam and only one type of low-affinity site (diazepam-binding sites) is involved in binding. That can be explained assuming an overlapping sites.
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