Identification of a protein that purifies with the scrapie prion

Science. 1982 Dec 24;218(4579):1309-11. doi: 10.1126/science.6815801.


Purification of prions from scrapie-infected hamster brain yielded a protein that was not found in a similar fraction from uninfected brain. The protein migrated with an apparent molecular size of 27,000 to 30,000 daltons in sodium dodecyl sulfate polyacrylamide gels. The resistance of this protein to digestion by proteinase K distinguished it from proteins of similar molecular weight found in normal hamster brain. Initial results suggest that the amount of this protein correlates with the titer of the agent.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brain / pathology*
  • Brain Chemistry
  • Centrifugation, Density Gradient
  • Cricetinae
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidase K
  • Endopeptidases / metabolism
  • Molecular Weight
  • Nerve Tissue Proteins / isolation & purification*
  • Prions / growth & development
  • Scrapie / pathology*
  • Sheep
  • Virus Activation


  • Nerve Tissue Proteins
  • Prions
  • Endopeptidases
  • Endopeptidase K