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December 24, 1982Science1,274 citations

Identification of a Protein That Purifies with the Scrapie Prion

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DBDavid C. BoltonMMMichael P. McKinleySPStanley B. Prusiner

Key Points

  • To identify and characterize specific proteins associated with purified scrapie prions from infected brain tissue.
  • Prion fractions were purified from scrapie-infected hamster brain tissue and compared against equivalent fractions from uninfected control brains.
  • Proteins were resolved using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and tested for susceptibility to proteinase K digestion.
  • A unique protein with an apparent molecular size of 27,000 to 30,000 daltons was identified in scrapie-infected fractions but was absent in uninfected fractions.
  • The identified protein demonstrated resistance to proteinase K digestion, distinguishing it from normal brain proteins of similar molecular weight.
  • Abundance of this protease-resistant protein correlated directly with the infectious titer of the scrapie agent.

Abstract

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.

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Cite This Study

Bolton et al. (1982) studied this question.

synapsesocial.com/papers/69ff926510d6befb25774c7ahttps://doi.org/10.1126/science.6815801
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