Abstract
We report a novel enzymatic method by which an E. coli produced precursor to human growth hormone (hGH) can be converted to authentic hGH. The hGH precursor contains an aminoterminal extension that is removed in vitro by the enzyme dipeptidylaminopeptidase I (DAP I). The aminoterminal extension has been tailored to allow the use of very specific purification steps. The highly purified hGH is indistinguishable from the 22K fraction of pituitary human growth hormone and shows full biological activity. In addition, the protein is overproduced in E. coli in a soluble form, obviating the use of chaotropic agents in its purification. The process may be used whenever the resulting product is a protein with proline as the second or third amino acid.
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Dalbøge, H., Dahl, HH., Pedersen, J. et al. A Novel Enzymatic Method for Production of Authentic hGH from an Escherichia Coli produced hGH–Precursor. Nat Biotechnol 5, 161–164 (1987). https://doi.org/10.1038/nbt0287-161
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DOI: https://doi.org/10.1038/nbt0287-161