Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis


Autoria(s): Lindae, Antje; Eberle, Raphael J.; Caruso, Icaro P.; Coronado, Monika A.; Moraes, Fabio R. de; Azevedo, Vasco; Arni, Raghuvir K.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

21/10/2015

21/10/2015

01/08/2015

Resumo

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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. (C) 2015 Elsevier Inc. All rights reserved.

Formato

15-20

Identificador

http://www.sciencedirect.com/science/article/pii/S1046592815000868

Protein Expression And Purification. San Diego: Academic Press Inc Elsevier Science, v. 112, p. 15-20, 2015.

1046-5928

http://hdl.handle.net/11449/128845

http://dx.doi.org/10.1016/j.pep.2015.04.006

WOS:000355572200003

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Protein Expression And Purification

Direitos

closedAccess

Palavras-Chave #C. pseudotuberculosis #Cold shock protein #Spectroscopic methods #Secondary structure #Folding and refolding proteins
Tipo

info:eu-repo/semantics/article