Abstract
The recombinant production of proteins leads to inclusion bodies which contain aggregated proteins in active, partially active, and inactive conformational states. These aggregated proteins must be extracted from the inclusion bodies, unfolded, and carefully refolded to the active and the stable conformational state. Mechanistic models for protein refolding are briefly presented. Different strategies and protocols are presented that lead to the active and stable protein conformational state. The techniques presented include chaperonin-assisted refolding, amino acid substitution, polyethylene glycolassisted refolding, protein refolding in reverse micelles, and antibody-assisted refolding of proteins. The techniques presented together provide a reasonable framework of the state-of-the-art and may be carefully applied to the bioseparation of other proteins and biological macromolecules of interest. (c) 1995 John Wiley & Sons, Inc.
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