High-level production of human growth hormone in Escherichia coli by a simple recombinant process

Nam Kyu Shin, Dae Young Kim, Chul Soo Shin, Min Sun Hong, Jeewon Lee, Hang Cheol Shin

Research output: Contribution to journalArticlepeer-review

47 Citations (Scopus)


Procedures have been devised for producing in Escherichia coli high yields of purified recombinant human growth hormone (hGH), by utilizing N-terminal pentapeptide sequence of human tumor necrosis factor-alpha, histidine tag and enterokinase cleavage site as a fusion partner. The fusion protein was produced as a soluble protein at the beginning of gene expression, but progressively became insoluble in Escherichia coli cytoplasm. The insoluble protein was solubilized by simple alkaline pH shift and purified to near homogeneity by Ni2+-chelated affinity chromatography. Following specific enterokinase cleavage, the recombinant hGH was purified by one-step anion exchange chromatography. The ease and speed of this recombinant process, as well as the high productivity, makes it adaptable to the large-scale production of hGH. Moreover, the highly efficient fusion partner could be applied to the production of other therapeutically important proteins. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)143-151
Number of pages9
JournalJournal of Biotechnology
Issue number2
Publication statusPublished - 1998 Jun 30
Externally publishedYes

Bibliographical note

Funding Information:
We are grateful to Dr B.-L. Seong in virology laboratory for providing recombinant enterokinase and for helpful discussions. This work was supported by Hanil Synthetic Fiber.


  • Chromatography
  • Escherichia coli
  • Human growth hormone

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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