| Project/Area Number |
08555183
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
化学工学一般
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| Research Institution | Osaka University |
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Principal Investigator |
KUBOI Ryoichi Prof., Grad.Sch.of Pharm., Osaka University, 大学院・基礎工学研究科, 教授 (40029567)
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| Co-Investigator(Kenkyū-buntansha) |
MANDAI Osabumi Manager, Murata Co.Ltd., 多層商品部, 部長
SHIOMORI Koichiro Res.Assoc., Fac.of Eng., Miyazaki University, 工学部, 助手 (80235506)
HIRAI Takayuki Assoc.Prof., Grad.Sch.of Eng.Sci., Osaka University, 大学院・基礎工学研究科, 助教授 (80208800)
TSUCHIDO Tetsuaki Prof., Fac.of Eng., Kansai University, 工学部, 教授 (50029295)
AZUMA Jyunichi Prof., Grad.Sch.of Eng.Sci., Osaka University, 大学院・薬学研究科, 教授 (30144463)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥7,700,000 (Direct Cost: ¥7,700,000)
Fiscal Year 1997: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1996: ¥6,200,000 (Direct Cost: ¥6,200,000)
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| Keywords | Stress Response / Bio-Separation / Reverse Micelle / Percolation / Refolding / Protein / Hydrophobic Interaction / Liposome / 分離・精製 / 分子集合体 / 膜透過 / 機能材料 / 会合コロイド / シャペロニン / 疎水性 |
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| Research Abstract |
The stress responsive functions, for example synthesis of specific proteins including a set of heat shock proteins, refolding of damaged proteins, translocation arid release of proteins across membranes, and formation of protein aggregates in an inert insoluble form etc., of biological nano-colloid such as cells, membranes, and proteins have been quantitatively analyzed by using the percolation method, aqueous two-phase partitioning method, and immobilized liposome chromatographyin the various levels focusing on the transient and weak molecular interactions between proteins and lipid membranes or reverse micelles under various stress conditions. It was found that the formation of a new transient structure between partly denatured proteins and reverse micelles or liposomes played the key role in the above stress resposive functions. It was found to be driven by the fluidity of nano-colloidal interface combined with the transient hydrophobic interaction between them and could be mediated and controlled by kinds of stressors, their combinations, and stress levels. These quantitative results have been successfully utilized for the design and development of novel and efficient protein refolding and bio-separation processes.
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