Production of Recombinant Chicken Glucagon Using E. coli

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概要

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• Recombinant chicken glucagon was successfully produced with a high level of expression in E. coli as a fusion protein with maltose-binding protein (MBP). The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from MBP-glucagon fusion protein with BLase that specifically cleaves the peptide bond on the carboxyl side of the glutamic acid residue. The resulting glucagon was purified to homogeneity by a combination of reverse-phase HPLC and ion-exchange HPLC, and its structure was confirmed by amino acid composition analysis. The overall yield of the recombinant glucagon was approximately 3.9mg from 1l of culture. According to its ability to stimulate lipolysis in chicken adipocytes, it was shown that recombinant chicken glucagon possesses biological activity.

著者

• HASEGAWA Shin

  Graduate School of Agricultural Science, Kobe University

• HONDA Kazuhisa

  Central Research Institute, Itoham food Inc.

• Motoki Tohru

  Graduate School Of Agricultural Science Kobe University

• KAMISOYAMA Hiroshi

  Faculty of Agriculture, Kagawa University

• YAGI Ken

  Graduate School of Science and Technology, Kobe University

• ISHIWATA Hiroko

  Faculty of Agriculture, Tohoku University

• FUJII Norihisa

  Graduate School of Science and Technology, Kobe University

• FURUYA Norihiko

  Faculty of Agriculture, Niigata University

• Tamaki Mikio

  Shionogi Research Laboratories Shionogi & Co. Ltd.

• Fujii Norihisa

  Graduate School Of Science And Technology Kobe University

• HONDA Kazuhisa

  Central Research Institute, Itoham Food Inc

• TAMAKI Mikio

  Shionogi Research Laboratories, Shionogi and Co., Ltd

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