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- W2004477360 abstract "The abnormal prion protein (PrPSc: scrapie-associated prion protein) is considered to be included in the group of infectious agents of transmissible spongiform encephalopathies. Since PrPSc is highly resistant to normal sterilization procedures, the decontamination of PrPSc is a significant public health issue. Tk-subtilisin is a subtilisin-like serine protease identified from a hyperthermophilic archaeon Thermococcus kodakarensis KOD1. Among the subtilisin family of proteases, Tk-subtilisin has significant high heat stability with its highest specific activity at 90°C and a half-life of 50 min at 100°C. In the present study, a hyper-thermostable protease, Tk-subtilisin, was used to degrade PrPSc. Although PrPSc is known to be resistant toward proteolytic enzymes, Tk-subtilisin was able to degrade PrPSc under extreme conditions. The level of PrPSc in brain homogenates was found to decrease significantly in vitro following Tk-subtilisin treatment at 100°C, whereas some protease resistant fractions remain after proteinase K treatment. Rather small amounts of Tk-subtilisin were required to degrade PrPSc at 100°C and pH 8.0. In addition, Tk-subtilisin was observed to degrade PrPSc in the presence of sodium dodecyl sulfate or other industrial surfactants. Although several proteases degrading PrPSc have been reported, practical decontamination procedures using enzymes are not available. This report aims to provide basic information for the practical use of a proteolytic enzyme for PrPSc degradation." @default.
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- W2004477360 date "2015-01-01" @default.
- W2004477360 modified "2023-09-28" @default.
- W2004477360 title "Proteolysis of Abnormal Prion Protein with a Thermostable Protease from a Hyper-Thermophilic Archaeon Thermococcus Kodakarensis Kod1" @default.
- W2004477360 doi "https://doi.org/10.1016/j.bpj.2014.11.2915" @default.
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