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  • Title: Purification and partial characterization of coxsackievirus B3 2A protease expressed in Escherichia coli.
    Author: Maghsoudi N, Khodagholi F, Sadjadi M, Zeinodini M, Sabbaghian M.
    Journal: Int J Biol Macromol; 2008 Oct 01; 43(3):238-44. PubMed ID: 18590760.
    Abstract:
    Reported here is the overexpression, purification and partial characterization of recombinant coxsakievirus B3 2A protease (CVB3 2Apro) from bacterial cells transformed with a plasmid containing the CVB3 2Apro cDNA sequences. The structural investigation showed that the protein contains mostly beta-strand elements and requires Zn2+ ions as a structural component which appeared to be inhibitory if added exogenously. The purified enzyme activity was optimal at 4 degrees C and had a short half-life at physiological temperature. This feature can be the result of the presence of a high content of beta-structure and also hydrophobic residues in its structure.
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