Chromatography with the use of immobilized bovine serum albumin as a stationary phase and aqueous buffer systems as eluents has proved to be a highly selective method, capable of separating structurally very closely related compounds. Retention can be effectively regulated by changes in at least three independent parameters of the mobile phase, which may be used for an optimization of separation factors. Particularly, the enantioselective properties of the chiral stationary phase have been demonstrated to be useful for the analytical resolution of a variety of racemates into enantiomers. From the variation of the retention behaviour with substituent effects, as well as the mobile phase composition, some indications regarding the molecular interaction forces regulating the substrate-protein equilibria have been obtained.
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