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Purification of Urease from Pleurotus sajor-caju. Characterisation of GTPase Activity of UreG and Biochemical Properties of the enzyme

Antik K. Bose ABSTRACT

Biochemical properties of urease obtained from fruiting body extract of Pleurotus sajorcaju have been described. The enzyme was purified 3176.623 fold by CM-cellulose, DEAEcellulose and Sephadex G-200 column chromatography. The molar mass estimated by Sephadex G-200 was 510KD and saccharide content was 4%. 6% SDS-PAGE of purified urease showed subunits UreA/B homodimer (28.8 KD ), UreC (150 KD), UreD (104 KD), UreE (21.5 KD), UreF (102 KD) and UreG (103KD). GTPase activity of UreG was characterized with KM, Vmax & Kcat to be 2.6mM, 1.1 mol GTP hydrolyzed/ min and 0.27 min-1. The enzyme hydrolyzed urea with KM and Vmax to be 1.85mM and 64.51 mol NH3 C and 7.4 respectively. The enzyme 2+ 2+ 2+ activity was enhanced by Ca (2.94%), 5-10 mM, Mn ( 2.67-52.406%), 20-50mM Ni (2.6-6.93% ) and 5-10mM Mncl2 ( 0.58- 8.02% ). The enzyme showed product inhibition by NH4+. Competitive inhibition by thiourea and uncompetitive inhibition by NaF were also studied. Amino acids at the active site have been identified to be Histidine and Aspartic acid using DEPC and Diazomethane with EDAC

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