Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
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چکیده
منابع مشابه
Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis.
Scrapie prion infectivity can be enriched from hamster brain homogenates by using limited proteolysis and detergent extraction. Purified fractions contain both scrapie infectivity and the protein PrP 27-30, which is aggregated in the form of prion rods. During purification, PrP 27-30 is produced from a larger membrane protein, PrPSc, by limited proteolysis with proteinase K. Brain homogenates f...
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In the course of scrapie, a transmissible spongiform encephalopathy caused by an unconventional agent, a normal cellular protein is converted to an abnormal form that copurifies with infectivity and aggregates to form deposits of amyloid. We have used immunocytochemistry and methods that enhance detection of amyloidogenic proteins to investigate the types of cells in the central nervous system ...
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Purified prion proteins and scrapie infectivity copartition into liposomes.
Considerable evidence indicates that the scrapie prion protein (PrP 27-30) is required for infectivity. Aggregates of PrP 27-30 form insoluble amyloid rods that resist dissociation by nondenaturing detergents. Mixtures of the detergent cholate and phospholipids were found to solubilize purified PrP 27-30 in the form of detergent-lipid-protein complexes. Removal of the cholate by dialysis result...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1991
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.65.3.1340-1351.1991