Optimization of production of recombinant human growth hormone in Escherichia coli

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.
• Key words: E.coli strain, ELISA, recombinant human growth hormone, recombinant protein expression, western blotting