Purification, and Properties of a Bovine Uricase

Muhammad   I.   Rajoka; Munazza      Mehraj; Muhammad   W.   Akhtar; Muhammad   A.   Zia

doi:10.2174/092986606775974366

Abstract

Uricase from bovine kidney, purified to homogeneity level, had a molecular weight of 70 kDa. The apparent Km and Vmax 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 (Δ H*) and entropy of activation (Δ S*) for uricase activity were lower than those reported for some thermostable enzymes.

Keywords: Bovine uricase, enthalpy, entropy, kinetics and thermodynamics, temperature inactivation

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Protein & Peptide Letters

Title: Purification, and Properties of a Bovine Uricase

Volume: 13 Issue: 4

Author(s): Muhammad I. Rajoka, Munazza Mehraj, Muhammad W. Akhtar and Muhammad A. Zia

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Keywords: Bovine uricase, enthalpy, entropy, kinetics and thermodynamics, temperature inactivation

Abstract: Uricase from bovine kidney, purified to homogeneity level, had a molecular weight of 70 kDa. The apparent Km and Vmax 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 (Δ H*) and entropy of activation (Δ S*) for uricase activity were lower than those reported for some thermostable enzymes.

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Rajoka I. Muhammad, Mehraj Munazza, Akhtar W. Muhammad and Zia A. Muhammad, Purification, and Properties of a Bovine Uricase, Protein & Peptide Letters 2006; 13 (4) . https://dx.doi.org/10.2174/092986606775974366