Halophilic β-lactamase as a new solubility- and folding-enhancing tag protein: Production of native human interleukin 1α and human neutrophil α-defensin

Applied Microbiology and Biotechnology

Volumn 86, Issue 2, 2010, Pages 649-658

  Tokunaga, Hiroko ^a   Saito, Shoko ^a,b   Sakai, Kazuki ^a   Yamaguchi, Rui ^a   Katsuyama, Iwao ^b   Arakawa, Tomohiro ^c   Onozaki, Kikuo ^c   Arakawa, Tsutomu ^d   Tokunaga, Masao ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b Epoch Medical International Inc (EMI)   (Japan)

^c NAGOYA CITY UNIVERSITY   (Japan)

^d Alliance Protein Laboratory   (United States)

Author keywords

Defensin; Lactamase; Folding enhancing tag; Halophilic; Interleukin 1 ; Solubility enhancing tag

Indexed keywords

ACIDIC AMINO ACIDS; AMINO ACID COMPOSITIONS; AQUEOUS SOLUBILITY; BIOLOGICAL ACTIVITIES; DEFENSINS; E. COLI; FOLDING-ENHANCING TAG; FUSION PARTNERS; FUSION PROTEINS; HETEROLOGOUS PROTEINS; HIGH SOLUBILITY; HUMAN INTERLEUKIN; HUMAN NEUTROPHIL; INTERLEUKIN-1; LACTAMASES; MODERATE HALOPHILE; NEGATIVE CHARGE; NEUTRAL PH; PERIPLASMIC SPACE; PROTEIN AGGREGATION; PROTEIN REFOLDING; REFOLDING EFFICIENCY; SOLUBLE EXPRESSION; UREA TREATMENT;

AMINO ACIDS; CATALYSTS; CYTOLOGY; ENZYMES; ESCHERICHIA COLI; GENE EXPRESSION; ORGANIC ACIDS; SOLUBILITY; UREA;

TERNARY SYSTEMS;

ALPHA DEFENSIN; BETA LACTAMASE; INTERLEUKIN 1ALPHA;

AGGREGATION; AMINO ACID; COLIFORM BACTERIUM; ENZYME; PEPTIDE; PH; PROTEIN; SOLUBILITY;

ARTICLE; ESCHERICHIA COLI; HALOPHILE; NONHUMAN;

ALPHA-DEFENSINS; BACTERIAL PROTEINS; BETA-LACTAMASES; ESCHERICHIA COLI; HUMANS; INTERLEUKIN-1ALPHA; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

ESCHERICHIA COLI;

EID: 77249093485     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2325-9     Document Type: Article

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