Purification and characterization of caprine kidney uricase, possessing novel kinetic and thermodynamic properties

Purified uricase from a caprine kidney, possessed K _m and V _max values of 1.1 mg ml⁻¹ and 3512 IU (mg protein)⁻¹ for uric acid hydrolysis, respectively. The optimum temperature and pH for catalytic activity were 40 °C and 8.5, respectively. The activation energy for formation of ES complex was 13.6 kJ mol⁻¹. Enthalpy (ΔH*), entropy of activation (ΔS*) and Gibbs free energy demand of uricase inactivation were 62.8 kJ mol⁻¹, −102 J mol⁻¹ K⁻¹ and 104.3 kJ mol⁻¹, respectively. Gibbs free enrgy demand for substrate binding and transition state stabilization were also determined which were comparable with those for themostable enzymes.