ArticleMolecular biotechnology2015
Cloning, expression, and purification of a synthetic human growth hormone in Escherichia coli using response surface methodology.
Article in Molecular biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 30 citations in OpenAlex.
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- Prokaryotic Expression, Purification, and Antibacterial Activity of the Hepcidin Peptide of Crescent Sweetlips (Current issues in molecular biology · 2023Article
- Cloning, Expression, and Purification of the Human Synthetic Survivin Protein in Escherichia coli Using Response Surface Methodology (RSM).Molecular biotechnology · 2023Article
- Generation of a recombinant version of a biologically active cell-permeant human HAND2 transcription factor from E. coli.Scientific reports · 2022Article
- Identification of Optimal Expression Parameters and Purification of a Codon-Optimized Human GLIS1 Transcription Factor from Escherichia coli.Molecular biotechnology · 2022Article
- Optimization of Expression and Purification of Schistosoma mansoni Antigens in Fusion with Rhizavidin.Molecular biotechnology · 2021Article
- Generation of a Recombinant Stem Cell-Specific Human SOX2 Protein from Escherichia coli Under Native Conditions.Molecular biotechnology · 2021Article
- Soluble expression, purification, and secondary structure determination of human MESP1 transcription factor.Applied microbiology and biotechnology · 2021Article
- Codon Optimization, Cloning, Expression, Purification, and Secondary Structure Determination of Human ETS2 Transcription Factor.Molecular biotechnology · 2020Article
- Stepwise optimization of recombinant protein production in Escherichia coli utilizing computational and experimental approaches.Applied microbiology and biotechnology · 2020Review
- Optimization and scale-up production of Zika virus ΔNS1 in Escherichia coli: application of Response Surface Methodology.AMB Express · 2019Article
- High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter.Bioengineered · 2017Article
- Identification of Novel Components Influencing Colonization Factor Antigen I Expression in Enterotoxigenic Escherichia coli.PloS one · 2015Article
- A Novel Strategy for Enhance Potentiation of Meglumine antimoniate againstIranian journal of parasitologyArticle
- Evaluation of Recombinant Human Growth Hormone Secretion inAvicenna journal of medical biotechnologyArticle
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this study was to achieve high-level production of the human growth hormone (hGH) in the prokaryotic expression system. In this regard, we performed cloning, expression, and purification of a synthetic hGH gene in BL21 (DE3) strain of E. coli. The hGH production was determined by SDS-PAGE and western blotting techniques, and then the protein concentration was determined by the Bradford assay. To gain insight into the effect of different nutrients on the growth of E. coli and hGH production, in a preliminary assessment nine different types of the basal medium were analyzed. The highest growth of E. coli and hGH production were observed in TB and SOB media. Accordingly, design of experiments was employed for screening the most significant nutrients, and central composite face design was applied for the optimization. The optimum medium consisted of yeast extract (10 g/L), tryptone (10 g/L), and K2HPO4 (2 g/L). The optimum hGH concentration was 391 mg/L, which was 3-fold higher than the hGH concentration in the LB basal medium (119 mg/L). This production rate is the highest hGH concentration reported in the IPTG-inducible expression systems.
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