A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express.
International audience 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 contaminat...
Published in: | Protein Expression and Purification |
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Format: | Article in Journal/Newspaper |
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2015
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Online Access: | https://hal.inrae.fr/hal-02635260 https://hal.inrae.fr/hal-02635260/document https://hal.inrae.fr/hal-02635260/file/1-s2.0-S1046592815000108-main_1.pdf https://doi.org/10.1016/j.pep.2015.01.009 |
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ftccsdartic:oai:HAL:hal-02635260v1 2023-05-15T14:45:32+02:00 A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. BELVAL, Lorène Marquette, Arnaud Mestre Artigues, Pedro-Felipe Piron, Marie-Christine Demangeat, Gerard Merdinoglu, Didier Chich, Jean-François Santé de la vigne et qualité du vin (SVQV) Institut National de la Recherche Agronomique (INRA)-Université de Strasbourg (UNISTRA) Institut de Chimie de Strasbourg Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) Département SPE 2015 https://hal.inrae.fr/hal-02635260 https://hal.inrae.fr/hal-02635260/document https://hal.inrae.fr/hal-02635260/file/1-s2.0-S1046592815000108-main_1.pdf https://doi.org/10.1016/j.pep.2015.01.009 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.pep.2015.01.009 info:eu-repo/semantics/altIdentifier/pmid/25655203 hal-02635260 https://hal.inrae.fr/hal-02635260 https://hal.inrae.fr/hal-02635260/document https://hal.inrae.fr/hal-02635260/file/1-s2.0-S1046592815000108-main_1.pdf doi:10.1016/j.pep.2015.01.009 PRODINRA: 304861 WOS: 000352121100005 PUBMED: 25655203 info:eu-repo/semantics/OpenAccess ISSN: 1046-5928 EISSN: 1096-0279 Protein Expression and Purification https://hal.inrae.fr/hal-02635260 Protein Expression and Purification, Elsevier, 2015, 109, pp.29-34. ⟨10.1016/j.pep.2015.01.009⟩ Arctic Express IMAC Cpn60 Recombinant protein [SDV]Life Sciences [q-bio] [SDV.BV]Life Sciences [q-bio]/Vegetal Biology info:eu-repo/semantics/article Journal articles 2015 ftccsdartic https://doi.org/10.1016/j.pep.2015.01.009 2021-12-19T01:16:20Z International audience 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. Article in Journal/Newspaper Arctic Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Arctic Protein Expression and Purification 109 29 34 |
institution |
Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
Arctic Express IMAC Cpn60 Recombinant protein [SDV]Life Sciences [q-bio] [SDV.BV]Life Sciences [q-bio]/Vegetal Biology |
spellingShingle |
Arctic Express IMAC Cpn60 Recombinant protein [SDV]Life Sciences [q-bio] [SDV.BV]Life Sciences [q-bio]/Vegetal Biology BELVAL, Lorène Marquette, Arnaud Mestre Artigues, Pedro-Felipe Piron, Marie-Christine Demangeat, Gerard Merdinoglu, Didier Chich, Jean-François A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
topic_facet |
Arctic Express IMAC Cpn60 Recombinant protein [SDV]Life Sciences [q-bio] [SDV.BV]Life Sciences [q-bio]/Vegetal Biology |
description |
International audience 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. |
author2 |
Santé de la vigne et qualité du vin (SVQV) Institut National de la Recherche Agronomique (INRA)-Université de Strasbourg (UNISTRA) Institut de Chimie de Strasbourg Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) Département SPE |
format |
Article in Journal/Newspaper |
author |
BELVAL, Lorène Marquette, Arnaud Mestre Artigues, Pedro-Felipe Piron, Marie-Christine Demangeat, Gerard Merdinoglu, Didier Chich, Jean-François |
author_facet |
BELVAL, Lorène Marquette, Arnaud Mestre Artigues, Pedro-Felipe Piron, Marie-Christine Demangeat, Gerard Merdinoglu, Didier Chich, Jean-François |
author_sort |
BELVAL, Lorène |
title |
A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
title_short |
A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
title_full |
A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
title_fullStr |
A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
title_full_unstemmed |
A fast and simple method to eliminate Cpn60 from functional recombinant proteins produced by E. coli Arctic Express. |
title_sort |
fast and simple method to eliminate cpn60 from functional recombinant proteins produced by e. coli arctic express. |
publisher |
HAL CCSD |
publishDate |
2015 |
url |
https://hal.inrae.fr/hal-02635260 https://hal.inrae.fr/hal-02635260/document https://hal.inrae.fr/hal-02635260/file/1-s2.0-S1046592815000108-main_1.pdf https://doi.org/10.1016/j.pep.2015.01.009 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
ISSN: 1046-5928 EISSN: 1096-0279 Protein Expression and Purification https://hal.inrae.fr/hal-02635260 Protein Expression and Purification, Elsevier, 2015, 109, pp.29-34. ⟨10.1016/j.pep.2015.01.009⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.pep.2015.01.009 info:eu-repo/semantics/altIdentifier/pmid/25655203 hal-02635260 https://hal.inrae.fr/hal-02635260 https://hal.inrae.fr/hal-02635260/document https://hal.inrae.fr/hal-02635260/file/1-s2.0-S1046592815000108-main_1.pdf doi:10.1016/j.pep.2015.01.009 PRODINRA: 304861 WOS: 000352121100005 PUBMED: 25655203 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.pep.2015.01.009 |
container_title |
Protein Expression and Purification |
container_volume |
109 |
container_start_page |
29 |
op_container_end_page |
34 |
_version_ |
1766316932532797440 |