Purification and characterization of a beta-glucuronidase present during embryogenesis of the mollusk Pomacea sp
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Wogelsanger O Pereira1, Ana K M Cruz, Elizabeth M M Albuquerque
1Departamento de Bioquímica, Centro de Biociencias, Universidade Federal do Rio Grande do Norte, 59072-970, Natal/RN, Brazil.
Abstract:
A beta-glucuronidase was purified from Pomacea sp. eggs by ammonium sulfate fractionation, DEAE-BioGel and Heparin-Sepharose chromatographies. This enzyme showed a Mr 180 kDa, with subunits of 90 kDa. The kinetic parameters were: pH 4.0, temperature 60 degrees C, Km 2.7 x 10(-6) and Vmax 15.3 microM/h, activator Mg+2, and inhibitor: lactone of D-saccharic acid. beta-glucuronidase is an exoglucuronidase involved in glycosaminoglycans metabolism with kinetics parameters similar to those found in mammals.
