| Project/Area Number |
25400426
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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 |
Biological physics/Chemical physics/Soft matter physics
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| Research Institution | Nagaoka University of Technology |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 蛋白質分解酵素 / 速度論的安定性 / 自己失活 / 熱測定 / 速度定数 / １次反応 / ２次反応 / 活性化エンタルピー / thermolysin / 立体構造変化 / savinase / 反応速度定数 / カルシウム濃度 / 酵素濃度 / タンパク質分解酵素 |
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| Outline of Final Research Achievements |
Although the kinetic stability of protease was traditionally analyzed by considering only the conformational change, a new kinetic model has been constructed with considering the self-digestion, Based on this method, the global analysis for the calorimetric data of proteases under various experimental conditions has been developed where the kinetic parameters were determined precisely. Using this method, kinetic stability of a metalloprotease, thermolysin (TLN) and a serine protease, savinase (SAV) has been analyzed successfully, and the effect of the inhibitor on the stability of TLN, and the effect of Ca ion on the stability of SAV, have been evaluated. Furthermore, the method has benn successfully applied to evaluate the kinetic stability of non-protease proteins consisting of multi-unit, such as calmodulin and amylomaltase, indicating the versatility of the method.
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