Dees C, German T L, Wade W F, Marsh R F
J Gen Virol. 1985 Apr;66 ( Pt 4):851-9. doi: 10.1099/0022-1317-66-4-851.
Previous studies have shown that the scrapie agent is highly membrane-associated. We examined the protein composition of gradient fractions enriched for large membrane vesicles prepared from scrapie-infected and uninfected hamster brain using various methods to extract membrane proteins. We also examined proteins in detergent-extracted membrane vesicles fractionated on CsCl gradients. No qualitative differences in protein composition were seen comparing scrapie-infected and uninfected samples by one-dimensional gel electrophoresis. Extraction of proteins from membrane vesicles by phenol, pyridine, perchloric acid or lithium diiodosalicylate also failed to reveal any unique proteins in scrapie-infected hamster brain. Attempts to solubilize hydrophobic proteins (proteolipids) from CsCl gradient fractions into organic solvents were unsuccessful. These findings indicate that any hydrophobic protein associated with the scrapie agent is not a proteolipid, and that the ability of solvents to reduce scrapie infectivity is not a result of extraction of a proteolipid.
先前的研究表明，羊瘙痒病病原体与膜高度相关。我们使用各种方法提取膜蛋白，检查了从感染羊瘙痒病和未感染羊瘙痒病的仓鼠脑中制备的富含大膜泡的梯度级分的蛋白质组成。我们还检查了在氯化铯梯度上分级分离的经去污剂提取的膜泡中的蛋白质。通过一维凝胶电泳比较感染羊瘙痒病和未感染羊瘙痒病的样品，未发现蛋白质组成上的定性差异。用苯酚、吡啶、高氯酸或二碘水杨酸锂从膜泡中提取蛋白质，也未能揭示感染羊瘙痒病的仓鼠脑中存在任何独特的蛋白质。尝试将来自氯化铯梯度级分的疏水蛋白（蛋白脂质）溶解到有机溶剂中未成功。这些发现表明，与羊瘙痒病病原体相关的任何疏水蛋白都不是蛋白脂质，并且溶剂降低羊瘙痒病感染力的能力不是提取蛋白脂质的结果。
