期刊论文详细信息
Brazilian Journal of Medical and Biological Research
Some physico-chemical parameters that influence proteinase K resistance and the infectivity of PrP Sc after high pressure treatment
P. Heindl2  A. Fernández García2  M. Büttner1  H. Voigt1  P. Butz2  B. Tauscher2  E. Pfaff1 
[1] ,Institute of Chemistry and Biology Federal Research Center for Nutrition and Food Karlsruhe,Germany
关键词: Native prion protein;    Pressure;    Inactivation;    pH;    Proteinase K sensitivity;    Prion conformation;   
DOI  :  10.1590/S0100-879X2005000800010
来源: SciELO
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【 摘 要 】

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 resistant and less infectious prions. However, opposite results were obtained after pressurizing native infectious prions at slightly acidic pH and in PBS of higher concentration. In this case an extensive fraction of native PrP Sc remained PK resistant after pressure treatment, indicating a protective effect possibly due to induced aggregation of prion proteins in such buffers.

【 授权许可】

CC BY   
 All the contents of this journal, except where otherwise noted, is licensed under a Creative Commons Attribution License

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