Abstract
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.
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