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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
Purification, and properties of a bovine uricase
Muhammad Ibrahim Rajoka1, Khalil-Ur- Rehman, Munazza Mehraj
1National Institute for Biotechnology and Genetic Engineering (NIBGE), Faisalabad, Pakistan. mirajoka@nibge.org
Abstract:
Uricase from bovine kidney, purified to homogeneity level, had a molecular weight of 70 kDa. The apparent K(m) and V(max) values for uric acid hydrolysis were 0.125 mM and 102 IU mg(-1) protein respectively. The activation energy requirement for uric acid hydrolysis by uricase and inactivation of enzyme were 11.6 and 14.5 kJ/M respectively. Both enthalpy (Delta H*) and entropy of activation (Delta S*) for uricase activity were lower than those reported for some thermostable enzymes.