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• W1974843553 abstract "Abstract The quantification of the binding strength between retinoic acid and the primary binding site of β‐lactoglobulin B by dynamic equilibrium affinity capillary electrophoresis (DE‐ACE) is described. Although the peaks for retinoic acid were broad, a distinctive shift in migration time could be observed upon complexation allowing the construction of a binding curve and three linearised plots. By performing the corresponding linear and non‐linear regression analyses, an apparent dissociation constant varying between 1.4 and 2.2 μM was measured in a 100 mM Tris‐acetate buffer at pH 8.2 with 30 mM Na 2 SO 4 and 1% EtOH as additives. The sample was prepared by adding a concentrated solution of retinoic acid in ethanol to the background electrolyte, such as to obtain a final 1% solution of ethanol and 5 μM retinoic acid in the buffer. It was shown that an MEKC‐based approach, attempted to improve the solubility of retinoic acid in the aqueous buffer, could not be used to perform a binding study." @default.
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• W1974843553 date "2003-01-01" @default.
• W1974843553 modified "2023-10-04" @default.
• W1974843553 title "Measurement of the binding of retinoic acid to β-lactoglobulin B by affinity capillary electrophoresis" @default.
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• W1974843553 doi "https://doi.org/10.1002/jssc.200390014" @default.
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