Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 43, Issue 3, Pages 238-244Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2008.05.008
Keywords
2A protease; coxsakievirus B3; purification
Funding
- Shahid Beheshti Medical University
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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. (C) 2008 Elsevier B.V. All rights reserved.
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