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Updated: Apr 14, 2026

Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis
Antje Lindae1, Raphael J Eberle1, Icaro P Caruso1
1Multiuser Center for Biomolecular Innovation, Departament of Physics, Universidade Estadual Paulista (UNESP), São Jose do Rio Preto-SP 15054-000, Brazil.
Abstract:
The gram-positive bacterium Corynebacterium pseudotuberculosis is the causative agent of different diseases that cause dramatically reduced yields of wool and milk, and results in weight loss, carcass condemnation and also death mainly in sheep, equids, cattle and goats and therefore globally results in considerable economical loss. Cold shock proteins are conserved in many bacteria and eukaryotic cells and they help to restore normal cell functions after cold shock in which some appear to have specific functions at normal growth temperature as well. Cold shock protein A from C. pseudotuberculosis was expressed in Escherichia coli and purified. The thermal unfolding/refolding process characterized by circular dichroism, differential scanning calorimetry and NMR spectroscopy techniques indicated that the refolding process was almost completely reversible.

