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Protein Engineering vol. 16 no. 7 pp. 535-541, 2003
© 2003 Oxford University Press

Immobilized oxidoreductase as an additive for refolding inclusion bodies: application to antibody fragments

Kouhei Tsumoto1, Mitsuo Umetsu, Hidenari Yamada, Takahiko Ito, Satoru Misawa and Izumi Kumagai1

Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Aoba-ku, Sendai 980-8579, Japan

1 To whom correspondence should be addressed. e-mail: tsumoto{at}mail.cc.tohoku.ac.jp; kmiz{at}mail.cc.tohoku.ac.jp

Three foldases—the apical domain of GroEL (mini-chaperone) and two oxidoreductases (DsbA and DsbC) from Escherichia coli—were studied in refolding a protein with immunoglobulin fold (immunoglobulin-folded protein) that had been produced as inclusion bodies in E.coli. The foldases promoted the refolding of single-chain antibody fragments from denaturant-solubilized and reduced inclusion bodies in vitro, and also effectively functioned as alternatives for labilizing agent and oxidizing reagent in the stepwise dialysis system. Immobilization of the oxidoreductases enhanced refolding and recovery of functional single-chain antibody in the dialysis system, suggesting that immobilized oxidoreductases can be used as an effective additive for refolding immunoglobulin-folded proteins in vitro.

Received April 7, 2003; revised June 5, 2003; accepted June 6, 2003.


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