A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles Protein Expression and Purification Year : 2015

A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express.

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.
Fichier principal
Vignette du fichier
1-s2.0-S1046592815000108-main_1.pdf (428.65 Ko) Télécharger le fichier
Origin Files produced by the author(s)
Loading...

Dates and versions

hal-02635260 , version 1 (27-05-2020)

Identifiers

Cite

Lorène Belval, Arnaud Marquette, Pedro-Felipe Mestre Artigues, Marie-Christine Piron, Gerard Demangeat, et al.. A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express.. Protein Expression and Purification, 2015, 109, pp.29-34. ⟨10.1016/j.pep.2015.01.009⟩. ⟨hal-02635260⟩
29 View
1950 Download

Altmetric

Share

Gmail Mastodon Facebook X LinkedIn More