Chaperone over-expression in Escherichia coli: Apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates

Protein Expression and Purification

Volumn 64, Issue 2, 2009, Pages 185-193

  Haacke, Annette ^a   Fendrich, Gabriele ^a   Ramage, Paul ^a   Geiser, Martin ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Co expression; Escherichia coli; Molecular chaperone; Protein folding; Protein kinases; Protein purification

Indexed keywords

CHAPERONE; PHOSPHOTRANSFERASE; RECOMBINANT PROTEIN;

ARTICLE; BIOSYNTHESIS; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; GENETICS; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SOLUBILITY;

CHROMATOGRAPHY, GEL; ESCHERICHIA COLI; MASS SPECTROMETRY; MOLECULAR CHAPERONES; PHOSPHOTRANSFERASES; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SOLUBILITY;

ESCHERICHIA COLI; EUKARYOTA;

EID: 58749091073     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.10.022     Document Type: Article

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