IDENTIFICATION OF A PROTEIN THAT PURIFIES WITH THE SCRAPIE PRION
IDENTIFICATION OF A PROTEIN THAT PURIFIES WITH THE SCRAPIE PRION
复制标题
DOI：
10.1126/science.6815801
复制
发表时间：
1982-01-01
期刊：
影响因子：
56.9
通讯作者：
PRUSINER, SB
中科院分区：
文献类型：
--
作者：
BOLTON, DC;MCKINLEY, MP;PRUSINER, SB
从感染瘙痒症的仓鼠大脑中纯化朊病毒，产生了一种在未感染大脑的类似部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迁移表观分子大小为 27,000-30,000 道尔顿。这种蛋白质对蛋白酶 K 消化的抵抗力使其与正常仓鼠大脑中发现的类似分子量的蛋白质不同。初步结果表明，这种蛋白质的含量与药剂的效价相关。
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.