Expression of human insulin-like growth factor I in bacteria: use of optimized gene fusion vectors to facilitate protein purification.

@article{Moks1987ExpressionOH,
  title={Expression of human insulin-like growth factor I in bacteria: use of optimized gene fusion vectors to facilitate protein purification.},
  author={Tomas Moks and Lars Bertil Abrahms{\'e}n and Erik Holmgren and M Bilich and Annika Ohrfelt Olsson and Mathias Uhl{\'e}n and G{\"u}nther Pohl and Catharina Sterky and H. Hultberg and Staffan Josephson},
  journal={Biochemistry},
  year={1987},
  volume={26 17},
  pages={5239-44}
}
Several fusions between the gene for human insulin-like growth factor I (IGF-I) and the genes for different IgG-binding fragments of staphylococcal protein A were assembled and compared regarding expression, secretion, and purification of the peptide hormone. After IgG affinity purification of the fusion proteins from the growth medium of Staphylococcus aureus or Escherichia coli, native IGF-I was released by cleavage of an Asn-Gly peptide bond with hydroxylamine. An optimized expression system… CONTINUE READING