Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Res Med Sci. 2012 Jul;17(7):681-5.

Optimization of production of recombinant human growth hormone in Escherichia coli.

Author information

  • 1Department of Biology, Faculty of Sciences, University of Isfahan, Hezar Jerib Street, Isfahan, Postcode: 81746-73695, Iran.

Abstract

BACKGROUND:

Human growth hormone (hGH) is a single-chain polypeptide that participates in a wide range of biological functions such as metabolism of proteins, carbohydrates and lipids as well as in growth, development and immunity. Growth hormone deficiency in human occurs both in children and adults. The routine treatment for this condition is administration of recombinant human growth hormone (rhGH) made by prokaryotes. Since nonglycosylated human growth hormone is a biologically active protein, prokaryotic expression systems are preferred for its production.

MATERIALS AND METHODS:

Different strains of E.coli were transformed by plasmid containing human growth hormone gene and cultured in different conditions. After induction by IPTG, recombinant human growth hormone production was assessed using ELISA, dot blotting and western blotting techniques.

RESULTS:

High levels of rhGH were produced using E.coli prokaryotic protein production system.

CONCLUSION:

This simple and cost effective production process could be recruited for large scale production of rhGH.

KEYWORDS:

E.coli strain; ELISA; recombinant human growth hormone; recombinant protein expression; western blotting

PMID:
23798931
[PubMed]
PMCID:
PMC3685787
Free PMC Article

Images from this publication.See all images (4)Free text

Figure 1
Figure 2
Figure 3
Figure 4
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for PubMed Central
    Loading ...
    Write to the Help Desk