| Literature DB >> 6431296 |
P E Bendheim, R A Barry, S J DeArmond, D P Stites, S B Prusiner.
Abstract
Scrapie is a slow infection of the nervous system which progresses in the absence of any apparent immune response. The recent development of a large-scale purification protocol for scrapie prions made it possible to obtain substantial quantities of electrophoretically purified prion protein (PrP 27-30) and we report here on the successful production of a rabbit antiserum to PrP 27-30. The antiserum reacted with PrP 27-30 and several lower molecular weight proteins as shown by Western blots; it did not react with protein preparations from uninfected brains. Discrete structures in the subependymal region of scrapie-infected hamster brains were stained immunocytochemically. These same structures also stained with Congo red dye and showed green birefringence with polarized light, a characteristic of purified prion rods. This staining pattern suggests that they are amyloid plaques.Entities:
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Year: 1984 PMID: 6431296 DOI: 10.1038/310418a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962