Abstract
The separation of amino acid enantiomers by means of ligand-exchange chromatography on an adsorbed chiral stationary phase was investigated under overloaded conditions. The selectivity of separation, the limit of mass loading and the peak shapes of enantiomers are strongly affected by the copper(II) concentration in the eluent. Under the optimum conditions it was possible to separate up to 2000 μg of amino acid on a 125 × 4 mm I.D. column. With increase in mass loading the peak shape of the enantiomers changed from symmetrical Gaussian into fronting and subsequently into trapezoidal. During this transformation, peak compression was observed. The complex changes in solute peak shape observed in ligand-exchange chromatography of amino acid enantiomers imply a complex form of adsorption isotherm in these systems.
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