IDENTIFICATION OF A PROTEIN THAT PURIFIES WITH THE SCRAPIE PRION

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 27,000-30,000 daltons in sodium dodecyl sulfate polyacrylamide gels. The resistance of this protein to digestion by proteinase K distinguished it from proteins of similar MW found in normal hamster brain. Initial results suggest that the amount of this protein correlates with the titer of the agent.