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Protein disaggregation and refolding using high hydrostatic pressure

✍ Scribed by David J Phelps; Lyndal K Hesterberg

Publisher
Wiley (John Wiley & Sons)
Year
2007
Tongue
English
Weight
83 KB
Volume
82
Category
Article
ISSN
0268-2575

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✦ Synopsis

Abstract

Production of recombinant proteins often leads to aggregate formation. These aggregates may make it impossible to solubilize the protein for downstream applications such as assay development or structural studies by X‐ray crystallography or nuclear magnetic resonance spectroscopy. High hydrostatic pressure technology has been developed which offers significant advantages over traditional methods of protein disaggregation and refolding. Pressure induced disruption of protein aggregates and subsequent refolding can take place at high concentrations in a single process step, without the need for high concentrations of chaotropic agents. Copyright Β© 2007 Society of Chemical Industry

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