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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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High pressure fosters protein refolding from aggregates at high concentrations.

High hydrostatic pressures (1-2 kbar), combined with low, nondenaturing concentrations of guanidine hydrochloride (GdmHCl) foster disaggregation and refolding of denatured and aggregated human growth hormone and lysozyme, and beta-lactamase inclusion bodies. One hundred percent recovery of properly folded protein can be obtained by applying pressures of 2 kbar to suspensions containing aggregates of recombinant human growth hormone (up to 8.7 mg/ml) and 0.75 M GdmHCl. Covalently crosslinked, insoluble aggregates of lysozyme could be refolded to native, functional protein at a 70% yield, independent of protein concentration up to 2 mg/ml. Inclusion bodies containing beta-lactamase could be refolded at high yields of active protein, even without added GdmHCl.[1]

References

  1. High pressure fosters protein refolding from aggregates at high concentrations. St John, R.J., Carpenter, J.F., Randolph, T.W. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
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