Identification of a protein that purifies with the scrapie prion
DC Bolton, MP McKinley, SB Prusiner - Science, 1982 - science.org
DC Bolton, MP McKinley, SB Prusiner
Science, 1982•science.orgPurification 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.
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.
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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