Efficient Production of Monoclonal Antibodies Using Heat Shock Proteins.

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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.