Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase.

@article{Hartman1992AffinityPO,
  title={Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase.},
  author={J Hartman and Pierre Daram and Raymond A Frizzell and T A Rado and Dale J. Benos and Eric Sorscher},
  journal={Biotechnology and bioengineering},
  year={1992},
  volume={39 8},
  pages={828-32}
}
Prokaryotic expression of polypeptides as fusion proteins with glutathione-S-transferase has recently been reported as a one-step means of purifying recombinant protein. The usefulness of the glutathione-S-transferase/glutathione-agarose system, however, is significantly limited by the frequent synthesis of recombinant proteins in insoluble form by Escherichia coli. We have found that for 5 separate fusion proteins containing glutathione-S-transferase and different domains of the large cystic… CONTINUE READING