| Literature DB >> 10773427 |
T G Baron1, J Y Madec, D Calavas, Y Richard, F Barillet.
Abstract
We compared the glycoform pattern of the abnormal prion protein (PrP(Sc)) detected by immunoblotting in 21 sheep with natural scrapie, from 21 different outbreaks identified in France since 1996, with a bovine spongiform encephalopathy (BSE)-infected sheep. All the natural scrapie isolates had a higher molecular mass of the unglycosylated PrP(Sc) than in BSE-infected sheep. In the latter case, this molecular mass appeared identical to that found in the CH 1641 experimental scrapie strain (type C pattern), whereas in natural scrapie cases it was similar to that found in the SSBP/1 experimental scrapie strains. These results suggest that all French natural scrapie isolates studied so far would belong, as SSBP/1, to the group of scrapie cases with type A electrophoretic pattern.Entities:
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Year: 2000 PMID: 10773427 DOI: 10.1016/s0304-3940(00)01047-8
Source DB: PubMed Journal: Neurosci Lett ISSN: 0304-3940 Impact factor: 3.046