Abstract
It was reported that PL promoter and alkaline phosphatase (phoA) signal peptide were used to construct secretory expression plasmid suitable to express glucagon and [Des-His1] glucagon in E. coli BL21 herein. Expression studies showed these two peptides could be expressed and secreted into the culture medium. The expression yield of recombinant glucagon reached 3.46 mg/L/OD600 unit of cells in shake flask. The yield of [Des-His1] glucagon was found to be higher than that of glucagon. In addition, some factors involved in secretion were studied too.
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Received: 26 September 2002 / Accepted: 24 October 2002
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Wen, C., Gan, R. & Zhu, S. Construction of Secretory Expression System Suitable to Express Glucagon Under the Control of PL Promoter. Curr Microbiol 47, 0180–0185 (2003). https://doi.org/10.1007/s00284-002-3988-y
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DOI: https://doi.org/10.1007/s00284-002-3988-y