Analysis of abnormal prion protein core structure by proteolysis at high temperature
| Project/Area Number |
15K07392
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
Koga Yuichi 大阪大学, 工学研究科, 准教授 (30379119)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | プロテアーゼ / 蛋白質工学 / PrP / Subtilisin / 耐熱性酵素 / 超好熱菌 / プリオン / プリオンタンパク質 |
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| Outline of Final Research Achievements |
A hyperthermostable protease, Tk-subtilisin, can degrade PrPSc. Scrapie-infected mouse brain homogenate ( RML strain ) was degraded by Tk-subtilisin under high-temperature condition and the degradation products were inoculated into culture cell. At high-temperature condition, Tk-subtilisin degraded PrP from RML homogenate, whereas proteinase K ( PK ) hardly degraded. In addition, Western blotting of the cell lysate inoculated the degradation product showed that the amount of PrPSc decreased significantly. Moreover, the signals of PrPSc were not observed when the concentration of Tk-subtilisin was increased. These results suggest that the combination of heat treatment and proteolysis by Tk-subtilisin is effective in reducing the infectivity titer of PrPSc.
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Report
(4 results)
Research Products
(14 results)
