Abstract
This paper studies the β-glucuronidase in the mollusk Pomacea sp. The β-glucuronidase was isolated 206-fold with a 1,5% yield and the cinetc parameters was: pH 5.0, 65°C, Km of 72 x 10-2 mM and molecular mass of 116 kDa. HPLC confirmed the purity. BaCl2 increased β-glucuronidase activity and SDS and NaH2PO4 inhibited completely.
Keywords: β- glucuronidase, glycosaminoglycans, high-performance liquid, chromatography (HPLC), Pomacea sp
Protein & Peptide Letters
Title: Isolation and Partial Characterization of A β-Glucuronidase of the Mollusk Pomacea sp.
Volume: 14 Issue: 10
Author(s): Maria Lucia Lira de Andrade, Vanessa Duarte de Morais and Joao Felipe de Sousa Filho
Affiliation:
Keywords: β- glucuronidase, glycosaminoglycans, high-performance liquid, chromatography (HPLC), Pomacea sp
Abstract: This paper studies the β-glucuronidase in the mollusk Pomacea sp. The β-glucuronidase was isolated 206-fold with a 1,5% yield and the cinetc parameters was: pH 5.0, 65°C, Km of 72 x 10-2 mM and molecular mass of 116 kDa. HPLC confirmed the purity. BaCl2 increased β-glucuronidase activity and SDS and NaH2PO4 inhibited completely.
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Cite this article as:
Lira de Andrade Lucia Maria, de Morais Duarte Vanessa and de Sousa Filho Felipe Joao, Isolation and Partial Characterization of A β-Glucuronidase of the Mollusk Pomacea sp., Protein & Peptide Letters 2007; 14 (10) . https://dx.doi.org/10.2174/092986607782541097
DOI https://dx.doi.org/10.2174/092986607782541097 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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