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| Heindl,P.; Fernández García,A.; Büttner,M.; Voigt,H.; Butz,P.; Tauscher,B.; Pfaff,E.. |
| Crude brain homogenates of terminally diseased hamsters infected with the 263 K strain of scrapie (PrP Sc) were heated and/or pressurized at 800 MPa at 60ºC for different times (a few seconds or 5, 30, 120 min) in phosphate-buffered saline (PBS) of different pH and concentration. Prion proteins were analyzed on immunoblots for their proteinase K (PK) resistance, and in hamster bioassays for their infectivity. Samples pressurized under initially neutral conditions and containing native PrP Sc were negative on immunoblots after PK treatment, and a 6-7 log reduction of infectious units per gram was found when the samples were pressurized in PBS of pH 7.4 for 2 h. A pressure-induced change in the protein conformation of native PrP Sc may lead to less PK... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Native prion protein; Pressure; Inactivation; PH; Proteinase K sensitivity; Prion conformation. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800010 |
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