Novel soluble expression technologies derived from unique properties of halophilic proteins

Applied Microbiology and Biotechnology

Volumn 88, Issue 6, 2010, Pages 1223-1231

  Tokunaga, Hiroko ^a   Arakawa, Tsutomu ^b   Tokunaga, Masao ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b Alliance Protein Laboratory   (United States)

Author keywords

Betalactamase; Fusion protein; Halophilic bacteria; Halophilic protein; Recombinant protein; Soluble expression

Indexed keywords

BETALACTAMASE; FUSION PROTEINS; HALOPHILIC BACTERIA; HALOPHILIC PROTEIN; RECOMBINANT PROTEIN; SOLUBLE EXPRESSION;

BACTERIOLOGY; CYTOLOGY; MAMMALS;

PROTEINS;

BACTERIAL PROTEIN; BETA LACTAMASE; HALOPHILIC PROTEIN; HYBRID PROTEIN; INTERLEUKIN 1ALPHA; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

BACTERIUM; BIOACCUMULATION; CYTOPLASM; ENZYME ACTIVITY; MAMMAL; MELTING; PHARMACEUTICAL INDUSTRY; PROTEIN; RECOMBINATION; SOLUTE; TEMPERATURE EFFECT;

CYTOPLASM; ESCHERICHIA COLI; EXPRESSION VECTOR; HALOPHILIC BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; SHORT SURVEY; THERMODYNAMICS;

BACTERIA; BETA-LACTAMASES; BIOTECHNOLOGY; CYTOPLASM; GENE EXPRESSION; HOT TEMPERATURE; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

MAMMALIA;

EID: 78649318193     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2832-8     Document Type: Short Survey

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