Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins.

@article{Schffner2001CosecretionOC,
  title={Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins.},
  author={Jochen Sch{\"a}ffner and Jeannette Winter and Rainer Rudolph and Elisabeth Schwarz},
  journal={Applied and environmental microbiology},
  year={2001},
  volume={67 9},
  pages={3994-4000}
}
Attempts were made to engineer the periplasm of Escherichia coli to an expression compartment of heterologous proteins in their native conformation. As a first approach the low-molecular-size additive L-arginine and the redox compound glutathione (GSH) were added to the culture medium. Addition of 0.4 M L-arginine and 5 mM reduced GSH increased the yield of a native tissue-type plasminogen activator variant (rPA), consisting of the kringle-2 and the protease domain, and a single-chain antibody… CONTINUE READING

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