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Production of Recombinant Proteins in the Ion-Deficient BL21(DE3) Strain of Escherichia coli in the Absence of the DnaK Chaperone
To eliminate unavoidable contamination of purified recombinant proteins by DnaK, we present a unique approach employing a BL21(DE3) ...dnaK strain of Escherichia coli. Selected representative purified proteins remained soluble, correctly assembled, and active. This finding establishes DnaK dispensab...
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Published in: | Applied and environmental microbiology 2009-06, Vol.75 (11), p.3803 |
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creator | Ratelade, Julien Miot, Marie-Caroline Johnson, Emmett Betton, Jean-Michel Mazodier, Philippe Benaroudj, Nadia |
description | To eliminate unavoidable contamination of purified recombinant proteins by DnaK, we present a unique approach employing a BL21(DE3) ...dnaK strain of Escherichia coli. Selected representative purified proteins remained soluble, correctly assembled, and active. This finding establishes DnaK dispensability for protein production in BL21(DE3), which is void of Lon protease, key to eliminating unfolded proteins. (ProQuest: ... denotes formulae/symbols omitted.) |
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Selected representative purified proteins remained soluble, correctly assembled, and active. This finding establishes DnaK dispensability for protein production in BL21(DE3), which is void of Lon protease, key to eliminating unfolded proteins. 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ispartof | Applied and environmental microbiology, 2009-06, Vol.75 (11), p.3803 |
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source | Open Access: PubMed Central; American Society for Microbiology Journals |
subjects | Bacterial proteins E coli Microbiology Proteases |
title | Production of Recombinant Proteins in the Ion-Deficient BL21(DE3) Strain of Escherichia coli in the Absence of the DnaK Chaperone |
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