Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.
Authors: Pereira, Wogelsanger O.; Cruz, Ana K.M.; Albuquerque, Elizabeth M.M.; Santos, Elizeu A.; Oliveira, Adeliana S.; Sales, Mauricio P.; Oliveira, Fernanda W.
Source: Protein and Peptide Letters, Volume 12, Number 7, October 2005 , pp. 695-700(6)
Publisher: Bentham Science Publishers
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.
Document Type: Review Article
Affiliations: LQFP-DBQ-CB Campus UFRN, 59072-970, Natal-RN, Brazil,
Publication date: October 1, 2005
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.