Technical refolding of proteins: Do we have freedom to operate?

Biotechnology Journal

Volumn 5, Issue 6, 2010, Pages 547-559

  Eiberle, Maria K ^a,c   Jungbauer, Alois ^b  

^a BOEHRINGER INGELHEIM RCV GMBH AND CO KG   (Austria)

^b UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^c Rentschler Biotechnologie GmbH   (Germany)

Author keywords

Escherichia coli; Inclusion bodies; On column; Recombinant proteins; Refolding

Indexed keywords

DENATURED PROTEINS; HIGH YIELD; HOST CELLS; HYDROPHOBIC PATCH; INCLUSION BODIES; LARGE BUFFER; LARGE-SCALE PRODUCTION; LOW CONCENTRATIONS; MISFOLDING; MIXING TIME; NATIVE CONFORMATION; ON-COLUMN REFOLDING; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN CONCENTRATIONS; RECOMBINANT PROTEIN; RECOMBINANT PROTEINS; REFOLDING; RENATURATION; SCALE-INVARIANT; TANK SIZE; THERAPEUTIC PROTEIN;

ESCHERICHIA COLI; PATENTS AND INVENTIONS;

PROTEINS;

ALGINIC ACID; ALPHA CYCLODEXTRIN; ARGININE; BETA CYCLODEXTRIN; BETA LACTAMASE; BUFFER; CYCLODEXTRIN; GAMMA CYCLODEXTRIN; GUANIDINE; UREA;

MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PURIFICATION; PROTEIN REFOLDING; PROTEIN RENATURATION; PROTEIN STABILITY; REVIEW; SOLUBILIZATION;

BIOTECHNOLOGY; ESCHERICHIA COLI; INCLUSION BODIES; PROTEIN FOLDING; PROTEIN STABILITY; RECOMBINANT PROTEINS; SOLUBILITY;

EID: 77953168318     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000001     Document Type: Review

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