1995 Fiscal Year Final Research Report Summary
Efficient Production of Monoclonal Antibodies Using Heat Shock Proteins.
| 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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| Project Period (FY) |
1994 – 1995
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| Keywords | Molecular chaperonin / Thermosstability / Inclusion body |
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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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