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

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

Volume: 12 Issue: 7

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

Affiliation:

Keywords: mollusk, pomacea sp, glucuronidase, embryo development

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.

Cite this article as:

Pereira O. Wogelsanger, Cruz K.M. Ana, Albuquerque M.M. Elizabeth, Santos A. Elizeu, Oliveira S. Adeliana, Sales P. Mauricio and Oliveira W. Fernanda, Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp., Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696055