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Protein & Peptide Letters

Author(s): Wogelsanger O. Pereira, Ana K.M. Cruz, Elizabeth M.M. Albuquerque, Elizeu A. Santos, Adeliana S. Oliveira, Mauricio P. Sales and Fernanda W. Oliveira

DOI: 10.2174/0929866054696055

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Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Page: [695 - 700] Pages: 6

  • * (Excluding Mailing and Handling)

Abstract

A β-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°C, Km 2.7 x 10-6 and Vmax 15.3 μM/h, activator Mg+2, and inhibitor: lactone of D-saccharic acid. β-glucuronidase is an exoglucuronidase involved in glycosaminoglycans metabolism with kinetics parameters similar to those found in mammals.

Keywords: mollusk, pomacea sp, glucuronidase, embryo development