Purification and partial characterization of coxsackievirus B3 2A protease expressed in Escherichia coli |
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Authors: | Maghsoudi Nader Khodagholi Fariba Sadjadi Mahnaz Zeinodini Mehdi Sabbaghian Marjan |
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Institution: | Neuroscience Research Center, Shahid Beheshti University, M.C., Tehran, Iran. |
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Abstract: | Reported here is the overexpression, purification and partial characterization of recombinant coxsakievirus B3 2A protease (CVB3 2A(pro)) from bacterial cells transformed with a plasmid containing the CVB3 2A(pro) cDNA sequences. The structural investigation showed that the protein contains mostly beta-strand elements and requires Zn(2+) 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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Keywords: | 2A protease Coxsakievirus B3 Purification |
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