Refolding of Proteins at High Concentration by Size Exclusion Chromatography

  • Guan, Yixin (Department of Chemical and Biochemical Engineering, Zhejiang University, Engineering Research Center, Dongseo University) ;
  • Gao, Yonggui (Department of Chemical and Biochemical Engineering, Zhejiang University, Engineering Research Center, Dongseo University) ;
  • Yao, Shanjing (Department of Chemical and Biochemical Engineering, Zhejiang University, Engineering Research Center, Dongseo University) ;
  • Cho, Man-Gi (Department of Chemical and Biochemical Engineering, Zhejiang University, Engineering Research Center, Dongseo University)
  • 발행 : 2002.09.28

초록

Renaturation of Lysozyme by size exclusion chromatography(SEC) to improve yield as well as the initial and final protein concentration has been studied in detail, Although urea decreases the rate of proteins refolding, it can suppress protein aggregation to sustain pathway of correct refolding at high protein concentration, and there existed an optimum urea concentration in renaturation buffer. Lysozyme was successfully refolded from initial protein concentration of up to 100mg/m1 by SEC, the yield was more than 40%. And the refolding of Interferon-${\gamma}$ was further investigated.

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