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  • Title: A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli.
    Author: Friedhoff P, Gimadutdinow O, Rüter T, Wende W, Urbanke C, Thole H, Pingoud A.
    Journal: Protein Expr Purif; 1994 Feb; 5(1):37-43. PubMed ID: 8167472.
    Abstract:
    Overproduction of the extracellular Serratia marcescens nuclease in Escherichia coli results in aggregation and sequestration of a large amount of the protein in inclusion bodies. Only a relatively small amount is secreted into the medium from which it can be purified following established procedures. The cell-associated insoluble protein can be solubilized in 6 M urea after breaking up the cells by sonication. Renaturation is achieved by dilution or dialysis. Subsequent phosphocellulose chromatography yields a homogeneous protein preparation which is shown by a variety of biochemical and biophysical analyses to be indistinguishable from conventionally prepared material. The high yield (> 10 mg/500-ml culture) and the ease of preparation (2 to 3 days) make this an attractive alternative to previously described procedures.
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