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Isolation and Partial Characterization of A β-Glucuronidase of the Mollusk Pomacea sp.

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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: Pomacea sp; chromatography (HPLC); glycosaminoglycans; high-performance liquid; β- glucuronidase

Document Type: Research Article


Publication date: 2007-10-01

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  • 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.
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