Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies |
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Authors: | Andrew D Guise Shuna M West Julian B Chaudhuri |
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Institution: | (1) School of Chemical Engineering, University of Bath, BA2 7AY UK |
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Abstract: | Eukaryotic proteins expressed inEscherichia coli often accumulate within the cell as insoluble protein aggregates or inclusion bodies. The recovery of structure and activity
from inclusion bodies is a complex process, there are no general rules for efficient renaturation. Research into understanding
how proteins fold in vivo is giving rise to potentially new refolding methods, for example, using molecular chaperones. In
this article we review what is understood about the main three classes of chaperone: the Stress 60, Stress 70, and Stress
90 proteins. We also give an overview of current process strategies for renaturing inclusion bodies, and report the use of
novel developments that have enhanced refolding yields. |
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Keywords: | Protein refolding molecular chaperones inclusion bodies multisubunits polyethylene glycol arginine |
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