THE MECHANISM OF RETENTION OF ENANTIOMERIC SOLUTES ON SILANIZED SILICA PLATES ELUTED WITH ALBUMIN SOLUTIONS

Charged and uncharged racemic solutes have been resolved on RP-18W/UV2 54 plates by eluting with solutions of different pH containing 2 % 2-p ropanol and high concentrations of bovine serum albumin (BSA). The ret ention in a reversed phase chromatographic system was regulated by the concentration of the protein in the mobile phase; for several solutes there was a linear relationship between R(F)/(1-R(F)) and albumin con centration. The total binding affinity of these compounds for BSA can be estimated from the quotient of the slope and the intercept. The rol e of BSA in the enantioseparation of the different racemates was discu ssed, and the results were compared with those obtained from columns c ontaining the protein immobilized on silica.