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Volume 12, Number 3—March 2006
Dispatch

Protease-resistant Prion Protein in Lymphoreticular Tumors of Variant Creutzfeldt-Jakob Disease Mice

Larisa Cervenakova*Comments to Author , Oksana Yakovleva*, and Carroll McKenzie*
Author affiliations: *American Red Cross, Rockville, Maryland, USA

Main Article

Figure

Immunoblot for protease-resistant prion protein (PrPres) from tissues of SJL/OlaHsd mouse infected with human variant Creutzfeld-Jakob disease (vCJD). Lanes 1–5 show representative pattern of extracted PrPres after digestion with proteinase K (100 μg/mL). Lane 1, brain tissue of vCJD patient (World Health Organization reference sample). Lanes 2–5, samples from vCJD mouse in which spontaneous lymphoreticular system tumors developed: lane 2, brain; lane 3, spleen with nodular tumors; lane 4, tissu

Figure. Immunoblot for protease-resistant prion protein (PrPres) from tissues of SJL/OlaHsd mouse infected with human variant Creutzfeld-Jakob disease (vCJD). Lanes 1–5 show representative pattern of extracted PrPres after digestion with proteinase K (100 μg/mL). Lane 1, brain tissue of vCJD patient (World Health Organization reference sample). Lanes 2–5, samples from vCJD mouse in which spontaneous lymphoreticular system tumors developed: lane 2, brain; lane 3, spleen with nodular tumors; lane 4, tissue from neoplastic lymph nodes; lane 5, neoplastic thymus. The amount of original tissue used for PrPres extraction is shown on the top. Samples were denatured by boiling for 10 min in Laemmli buffer containing 2% β-mercaptoethanol, resolved on NuPAGE 12% Bis-Tris gel (Invitrogen Life Technologies, Carlsbad, CA, USA), transferred to nitrocellulose membrane, and probed with anti-PrP monoclonal antibody 6D11 (dilution 1:5,000). Major glycoforms of PrPres are present as 3 bands corresponding to diglycosylated, monoglycosylated, and unglycosylated molecules.

Main Article

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