A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express.
Protein Expr Purif
; 109: 29-34, 2015 May.
Article
em En
| MEDLINE
| ID: mdl-25655203
ABSTRACT
A frequent problem of recombinant protein production is their insolubility. To address this issue, engineered Escherichiacoli strains like Arctic Express that produce an exogenous chaperone facilitating protein folding, have been designed. A drawback is the frequent contamination of the protein by chaperones. A simple method, using urea at a sub-denaturing concentration, allows unbinding of Cpn60 from expressed protein. This method was successfully used to purify 2 proteins, an enzyme and a viral protein. The enzyme was fully active. The nature of interaction forces between enzyme and Cpn60 was investigated. The method is likely applicable to purify other proteins.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bioquímica
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Proteínas Recombinantes
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Engenharia Genética
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Chaperonina 60
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Escherichia coli
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article