Bolton D C, McKinley M P, Prusiner S B
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.
从感染羊瘙痒病的仓鼠脑中纯化朊病毒，得到了一种在未感染脑的类似组分中未发现的蛋白质。该蛋白质在十二烷基硫酸钠聚丙烯酰胺凝胶中的表观分子量为27,000至30,000道尔顿。这种蛋白质对蛋白酶K消化的抗性使其与正常仓鼠脑中发现的分子量相似的蛋白质区分开来。初步结果表明，这种蛋白质的量与病原体的滴度相关。
