Development of an optimized refolding process for recombinant Ala–Glu–IGF-1

Denatured and reduced N-terminal extended insulin-like growth factor-1 (AE-IGF-1) was purified from Escherichia coli extracts and subjected to in vitro folding. The renaturation process was shown to be a function of the redox potential of the solution. Folding by different methods had no significant...

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Veröffentlicht in:	Protein engineering 1992-12, Vol.5 (8), p.797-806
Hauptverfasser:	Hejnaes, Kim Ry, Bayne, Stephen, Nørskov, Leif, Holmegaard, Hans, Sørensen, H.H., Thomsen, Johannes, Schäffer, Lauge, Wollmer, Axel, Skriver, Lars
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aminopeptidases - pharmacology Binding, Competitive Biological and medical sciences Circular Dichroism Conformational dynamics in molecular biology Cysteine Endopeptidases - genetics energy minimization Escherichia coli folding Fundamental and applied biological sciences. Psychology Humans Insulin-Like Growth Factor I - analogs & derivatives Insulin-Like Growth Factor I - drug effects Insulin-Like Growth Factor I - genetics Insulin-Like Growth Factor I - metabolism Models, Molecular Molecular biophysics molecular modelling Molecular Sequence Data Molecular Weight Peptide Mapping Protein Denaturation Protein Engineering Protein Folding Receptor, IGF Type 1 - metabolism recombinant human IGF-1 Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid
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