The expression of foreign proteins at high levels in E. coli often results in the formation of inclusion bodies composed of insoluble aggregates of the expressed protein. The inclusion bodies are recovered from bacterial lysates by centrifugation and are washed with Triton X-100 and EDTA to remove as much bacterial protein as possible from the aggregated foreign protein.To obtain soluble protein, the washed inclusion bodies are dissolved in denaturing agents and the released protein is then refolded by gradual removal of the denaturing reagents by dilution or dialysis. The procedure given here has been used to solubilize prorennin inclusion bodies. However, each protein may require a slightly different procedure, which must be determined empirically.
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