CHIRAL SEPARATIONS USING AN IMMOBILIZED PROTEIN-DEXTRAN POLYMER NETWORK IN AFFINITY CAPILLARY ELECTROPHORESIS

An improvement in affinity capillary electrophoresis (ACE) was achieved by covalently linking bovine serum albumin (BSA) to a high-molecular-mass dextran (M(r) 2 000 000) using cyanogen bromide. The efficiency of the binding reaction was greater than 99%, measured through quantitative separation of the protein and protein-dextran polymer network mixture on a bare capillary using capillary electrophoresis (CE). Baseline separation of leucovorin (LV) enantiomers was obtained under 9 min using a linear polyacrylamide-coated capillary (with an effective length of 20 cm) filled with the BSA-dextran polymer network. The present work offers several significant advantages over other approaches to ligand immobilization, and can be generally applied to a wide variety of ligand-substrate systems.