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Recovery of Soluble, Biologically Active Recombinant Proteins from Total Bacterial Lysates Using Ion Exchange Resin

Bio/Technology volume 6, pages 1214–1217 (1988)Cite this article

Abstract

Eucaryotic proteins expressed intracellularly in Escherichia coli are frequently sequestered in insoluble inclusion bodies that must be solubilized prior to protein purification. Treatment of bacterial lysates with ion exchange resin has been found to solubilize 3 different recombinant proteins: an SV40 T antigen peptide Th encompassing the DNA binding do main of the intact protein, human interleukin 2, and the retroviral v-myb oncoprotein. The well-defined activities of peptide Th and interleukin were recovered in whole or in part in the solubilized proteins. This procedure may be generally applicable to the purification of insoluble recombinant proteins from E. coli or other expression systems.

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Author notes

  1. Ellen Fanning: Corresponding author.

Authors and Affiliations

  1. Institute for Biochemistry, Karlstr. 23, 8000, München, 2, FRG

    Adolf Hoess, Avril K. Arthur & Ellen Fanning

  2. Botanical Institute, Menzinger Str. 67, 8000, München, 19, FRG

    Gerhard Wanner

Authors
  1. Adolf Hoess
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  2. Avril K. Arthur
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  3. Gerhard Wanner
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  4. Ellen Fanning
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Hoess, A., Arthur, A., Wanner, G. et al. Recovery of Soluble, Biologically Active Recombinant Proteins from Total Bacterial Lysates Using Ion Exchange Resin. Nat Biotechnol 6, 1214–1217 (1988). https://doi.org/10.1038/nbt1088-1214

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  • DOI: https://doi.org/10.1038/nbt1088-1214

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