Measurement of the binding of retinoic acid to β‐lactoglobulin B by affinity capillary electrophoresis

摘要: The quantification of the binding strength between retinoic acid and primary site p-lactoglobulin B by dynamic equilibrium affinity capillary electrophoresis (DE-ACE) is described. Although peaks for were broad, a distinctive shift in migration time could be observed upon complexation allowing construction curve three linearised plots. By performing corresponding linear non-linear regression analyses, an apparent dissociation constant varying 1.4 2.2 μM was measured 100 mM Tris-acetate buffer at pH 8.2 with 30 Na 2 SO 4 1 % EtOH as additives. sample prepared adding concentrated solution ethanol to background electrolyte, such obtain final 1% 5 buffer. It shown that MEKC-based approach, attempted improve solubility aqueous buffer, not used perform study.