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Volume 17, Number 1—January 2011

Research

Molecular Typing of Protease-Resistant Prion Protein in Transmissible Spongiform Encephalopathies of Small Ruminants, France, 2002–2009

Johann Vulin, Anne-Gaëlle Biacabe, Géraldine Cazeau, Didier Calavas, and Thierry BaronComments to Author 
Author affiliations: Author affiliation: Agence Nationale de Sécurité Sanitaire, Lyon, France

Main Article

Figure 3

Differences in molecular mass observed between protease-resistant prion protein in cattle bovine spongiform encephalopathy (BSE) and usual transmissible spongiform encephalopathy cases in small ruminants. Differential molecular mass was obtained by subtracting the molecular mass of the unglycosylated band of the cattle BSE control to that of the natural small ruminant isolate from an immunoblot detected by Bar233 antibody.

Figure 3. Differences in molecular mass observed between protease-resistant prion protein in cattle bovine spongiform encephalopathy (BSE) and usual transmissible spongiform encephalopathy cases in small ruminants. Differential molecular mass was obtained by subtracting the molecular mass of the unglycosylated band of the cattle BSE control to that of the natural small ruminant isolate from an immunoblot detected by Bar233 antibody.

Main Article

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