Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: Evidence that chaperone activity is the prime effect of thioredoxin

Journal of Molecular Biology

Volumn 357, Issue 1, 2006, Pages 49-61

  Jurado, Paola ^a   De Lorenzo, Víctor ^a   Fernández, Luis A ^a  

^a CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

Author keywords

Disulfide bonds; E. coli; Intrabodies; Protein folding; Recombinant antibodies

Indexed keywords

CHAPERONE; GLUTATHIONE OXIDOREDUCTASE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; OXIDOREDUCTASE; SIGNAL PEPTIDE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; THIOREDOXIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

ANTIBODY AFFINITY; ANTIBODY PRODUCTION; ANTIGEN BINDING; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SOLUBILITY; WILD TYPE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 33644759558     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.058     Document Type: Article

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