Yeast-derived recombinant human insulin-like growth factor I: production, purification, and structural characterization.

@article{Elliott1990YeastderivedRH,
  title={Yeast-derived recombinant human insulin-like growth factor I: production, purification, and structural characterization.},
  author={Steve Elliott and K D Fagin and Linda Owers Narhi and James Adam Miller and M H Jones and Raymond A. Koski and Mike Peters and Pei-Wen Hsieh and Rani Sachdev and Robert D Rosenfeld},
  journal={Journal of protein chemistry},
  year={1990},
  volume={9 1},
  pages={95-104}
}
Recombinant human insulin-like growth factor I (IGF-I) is efficiently expressed and secreted from Saccharomyces cerevisiae using a yeast alpha-factor leader to direct secretion. However, approximately 10-20% of the IGF-I was in a monomeric form, the remaining materials being disulfide-linked aggregates. When the purified material was subjected to reverse-phase high-performance liquid chromatography (rp-HPLC), it gave two doublet peaks, I and II. Upon reduction, doublet peaks I and II converged… CONTINUE READING

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