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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Purification, and Properties of a Bovine Uricase

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

Volume 13, Issue 4, 2006

Page: [363 - 368] Pages: 6

DOI: 10.2174/092986606775974366

Price: $65

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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