Rapid Purification of Recombinant Human Lipocortin-I Secreted from Saccharomyces cerevisiae

  • Chung, Bong-Hyun (Korea Research Institute of Bioscience and Biotechnology, P.O.Box 115, Yusong, Taejon 305-600) ;
  • Nam, Soo-Wan (Department of Microbiology, College of Natural Science, Dongeui University, Pusan 614-714)
  • Published : 2000.07.01

Abstract

Human lipocortin-I was expressed as a secretory product by Saccharomyces cerevisiae harboring an expression system consisting of GAL10 promoter, inulinase signal sequence and lipocortin-I terminator. Fed-batch fermentation was carried out to overproduce recombinant human lipocortin-I. The culture medium was desalted and concentrated by ultrafiltration, and then subjected to hydroxyapatite column chromatography. The lipocortin-I was purified to >98% purity by single-step hydroxyapatite column chromato-graphy. However, it was found that the purified lipocortin-I was a proteolytically-cleaved form which was cleaved immediately after the basic amino acid Lys26.

Keywords

References

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