| Project/Area Number |
06555247
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| Research Category |
Grant-in-Aid for Developmental Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
生物・生体工学
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| Research Institution | OSAKA UNIVERSITY |
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Principal Investigator |
IMANAKA Tadayuki Osaka University, Faculty of Engineering, Professor, 工学部, 教授 (30029219)
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| Co-Investigator(Kenkyū-buntansha) |
高木 昌宏 大阪大学, 工学部, 助教授 (00183434)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥4,500,000 (Direct Cost: ¥4,500,000)
Fiscal Year 1995: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1994: ¥3,100,000 (Direct Cost: ¥3,100,000)
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| Keywords | Molecular chaperonin / Thermosstability / Inclusion body / 熱ショックタンパク質 / 細胞内フォールディング / インクルージョンボディー / タンパク質フォールディイング / モノクローナル抗体 / シャペロニン / インクルジョンボディー / 巻き戻し |
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| Research Abstract |
Heat shock proteins (molecular chaperons) are proteins which take a role in proper folding of protein structures. The project was initiated to study role of these molecular chaeronins from both bacteria and hyperthermophilic archaea during protein folding process. We cloned groEL and groES genes from Bacilllus stearothermophilus and showed that the GroEL and ES proteins can enhance thermostability of alcohol dehyderogenase from Saccharomyces cerevisiae. The effect was more significant when molecular chaperon from hyperthermophile Pyrococcus sp.KOD1 was used. These data suggested that molecular chaperons are useful both in vitro stabilization and in vivo solublization of foreign proteins.
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