Production of recombinant mink growth hormone in E. coli

@article{Sereikaite2006ProductionOR,
  title={Production of recombinant mink growth hormone in E. coli},
  author={Jolanta Sereikaite and Alina Statkute and Mindaugas Morkunas and Kostas Radzevi{\vc}ius and Vitaliano Borromeo and Camillo Secchi and Vladas-Algirdas Bumelis},
  journal={Applied Microbiology and Biotechnology},
  year={2006},
  volume={74},
  pages={316-323}
}
Escherichia coli cells expressing mink (Mustela vison) growth hormone were grown in a batch fermentation process. The expression level was estimated to be 27% of the total cellular protein after 3 h of induction with 1 mM isopropyl β-d-thiogalactoside (IPTG). If the expression of mink growth hormone (mGH) was induced with 0.2 mM IPTG, the concentration of target protein was slightly lower and was found to be 23% at the same time after induction. mGH expressed as inclusion bodies was solubilized… CONTINUE READING
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References

Publications referenced by this paper.
Showing 1-10 of 37 references

Separation of recombinant porcine growth hormone monomer from dimer and other oligomers in production process from E . coli inclusion bodies

  • J Sereikaite, Bumelis V-A
  • Biologija
  • 2006

Influence of growth limiting factors on recombinant growth hormone expression in E . coli

  • M Morkunas, S Alisauskaite, J Sereikaite, Bumelis V-A
  • J Biotechnol
  • 2005

Refolding of porcine growth hormone from inclusion bodies of Escherichia coli

  • L Baranauskaite, J Sereikaite, G Gedminiene, Z Bumeliene, Bumelis V-A
  • Biocatal Biotransform
  • 2005

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