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. 2015 Aug 6;11(8):e1004977. doi: 10.1371/journal.ppat.1004977

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© 2015 Vidal et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 2 — Two representative brain homogenates (per group) from TgRab mice inoculated with different prion strains [cattle: BSE-L and BSE-C; mouse: RML and ME7; sheep: SSPB/1, sheep BSE-C and atypical scrapie; deer: CWD; rabbit: de novo–RaPrP^res (in vitro sample) and de novo–NZW (in vivo sample)] were digested with 100 μg/ml of proteinase K (PK) and analyzed by western blot using two different monoclonal antibodies (upper blot- 6H4 and lower blot– 12B2). Differential electrophoretic migrations and glycosylation patterns observed are consistent with the origin of the prion strains used for inoculation. Control NZW: Normal rabbit brain homogenate. MW: Molecular weight. Vertical lines separate blots with different exposition times.