NR AMQO

AU Winklhofer,K.F.; Hartl,F.U.; Tatzelt,J.

TI A sensitive filter retention assay for the detection of PrPsc and the screening of anti-prion compounds

QU FEBS Letters 2001 Aug 10; 503(1): 41-5

PT journal article

AB A hallmark of prion diseases is the accumulation of an abnormally folded prion protein, denoted PrPsc. Here we describe a new and highly sensitive method for the detection of PrPsc in brain and other tissue samples that utilizes both PrPsc diagnostic criteria in combination; protease resistance and aggregation. Upon filtration of tissue extracts derived from scrapie- or bovine spongiform encephalopathy-infected animals, PrPsc is retained and detected on the membranes. Laborious steps such as SDS-PAGE and Western blotting are avoided with concomitant gain in sensitivity and reliability. The new procedure also proved useful in a screen for anti-prion compounds in a scrapie-infected cell culture model.

MH Animal; Blotting, Western; Brain/metabolism; Cattle; Drug Evaluation, Preclinical/methods; Electrophoresis, Polyacrylamide Gel; Encephalopathy, Bovine Spongiform/metabolism; Mice; PrPsc Proteins/*analysis/antagonists & inhibitors/metabolism; Sensitivity and Specificity; Tumor Cells, Cultured

AD Department of Cellular Biochemistry, Max-Planck-Institut für Biochemie, D-82152, Martinsried, Germany.

SP englisch

PO Niederlande

EA pdf-Datei

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