Vitamin B2, also known as riboflavin (Rf), binds tightly to its carrier protein, riboflavin binding protein (RBP), under normal biological conditions. Rf can be removed from the RBP under acidic conditions, resulting in apo-RBP. The thermoodynamic parameters of Rf binding to RBP have been determined previously by several methods, including fluorimetry. The thermodynamics of the binding interaction of Rf to apo-RBP were analyzed by isothermal titration calorimetry (ITC) and compared to previous measurements by fluorimetry conducted in the 1980s. Titration data was simulated to determine complete thermodynamic parameters including ΔH, ΔS, and Kb.<br/>

Isothermal titration calorimetry (ITC) of vitamin B2 binding to apo- riboflavin binding protein

2019 Spring National Meeting

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