Barry R A, Vincent M T, Kent S B, Hood L E, Prusiner S B
Department of Neurology, University of California, San Francisco 94143.
J Immunol. 1988 Feb 15;140(4):1188-93.
The prion protein (PrP) 27-30 is the major macromolecular component in highly purified preparations of prions derived from scrapie-infected hamster brain. Immunoblotting studies demonstrated that this protein is generated by partial protease digestion of a larger precursor (PrPSc) with an apparent Mr of 33 to 35 kDa, and that a protease-sensitive cellular PrP isoform, designated PrPC, is present in normal hamster brain. To characterize the relationships among these proteins, ELISA and immunoblotting studies were undertaken with rabbit antisera raised against three synthetic PrP peptides. All three antisera were found to specifically react with the prion proteins, and failed to identify other lower or higher m.w. PrP proteins. Our results provide evidence that the primary structures of PrP 27-30, PrPSc, and PrPC are related; this conclusion supports molecular cloning studies indicating that these proteins are encoded by the same chromosomal gene.
朊病毒蛋白（PrP）27 - 30是从感染瘙痒病的仓鼠脑中高度纯化的朊病毒制剂中的主要大分子成分。免疫印迹研究表明，该蛋白是由一种表观分子量为33至35 kDa的较大前体（PrPSc）经部分蛋白酶消化产生的，并且在正常仓鼠脑中存在一种对蛋白酶敏感的细胞PrP异构体，称为PrPC。为了表征这些蛋白质之间的关系，使用针对三种合成PrP肽产生的兔抗血清进行了ELISA和免疫印迹研究。发现所有三种抗血清都能与朊病毒蛋白特异性反应，并且未能识别其他分子量更低或更高的PrP蛋白。我们的结果提供了证据表明PrP 27 - 30、PrPSc和PrPC的一级结构相关；这一结论支持了分子克隆研究，表明这些蛋白质由同一染色体基因编码。
