Surface supercharged human enteropeptidase light chain shows improved solubility and refolding yield

Protein Engineering, Design and Selection

Volumn 24, Issue 3, 2011, Pages 261-268

  Simeonov, Peter ^a   Berger Hoffmann, Renate ^a   Hoffmann, Ralf ^a   Sträter, Norbert ^a   Zuchner, Thole ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

enterokinase; human enteropeptidase; protein solubility; refolding yield; surface supercharging

Indexed keywords

BIOTECHNOLOGICAL APPLICATIONS; CYSTEINE RESIDUES; ENTEROKINASE; ENTEROPEPTIDASES; HEAT STABILITY; HIGH ACTIVITY; IMPROVED SOLUBILITY; LIGHT CHAIN; PROTEIN MODIFICATIONS; PROTEIN SOLUBILITY; PROTEIN SURFACE; REFOLDING; SERINE PROTEASE;

AMINO ACIDS; BIOTECHNOLOGY; ENZYME ACTIVITY; SOLUBILITY;

PROTEINS;

CYSTEINE; ENTEROPEPTIDASE; SERINE;

ARTICLE; ENZYME ACTIVITY; HEAT; LIGHT CHAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEIN STABILITY; SOLUBILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BIOCATALYSIS; CLONING, MOLECULAR; ENTEROPEPTIDASE; ENZYME STABILITY; ESCHERICHIA COLI; HOT TEMPERATURE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN REFOLDING; PROTEIN SUBUNITS; SOLUBILITY; STATIC ELECTRICITY;

EID: 79951925950     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq104     Document Type: Article

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