Dye-ligand chromatography

The affinity of two kinases for Blue Dextran was discovered in 1968 during gel permeation chromatography (1) and agarose electrophoresis (2). The observed interaction was mediated by the chromophore of Blue Dextran, Cibacron Blue F3G-A (3), which was postulated to bind to the supersecondary structure of certain enzymes known as the dinucleotide fold (4). Immobilized Cibacron Blue F3G-A replaced more expensive biological group-specific ligands in the affinity chromatographic purification of a wide variety of nucleotide-binding enzymes (5). The adsorbent was easier to synthesize, biochemically more stable, and had much higher capacities than the traditional nucleotide-based affinity matrices, making it more suitable for large-scale purifications.