High-level expression and characterization of a purified 142-residue polypeptide of the prion protein.

@article{Mehlhorn1996HighlevelEA,
  title={High-level expression and characterization of a purified 142-residue polypeptide of the prion protein.},
  author={Ingrid R. Mehlhorn and Darlene Groth and James Stoeckel and Barbara Moffat and Dorothea E Reilly and Daniel G. Yansura and W S Willett and Michael Baldwin and Robert Fletterick and Fred E. Cohen and Richard Vandlen and D. Henner and Stanley B Prusiner},
  journal={Biochemistry},
  year={1996},
  volume={35 17},
  pages={5528-37}
}
The major, and possible only, component of the infectious prion is the scrapie prion protein (PrPSc); the protease resistant core of PrPSc is PrP 27-30, a protein of approximately 142 amino acids. PrPSc is derived from the cellular PrP isoform (PrPC) by a post-transliatonal process in which a profound conformational change occurs. Syrian hamster (SHa) PrP genes of varying length ranging from the N- and C- terminally truncated 90-228 up to the full-length mature protein 23-231 were inserted into… CONTINUE READING
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