ArticlePloS one2014
Prokaryotic soluble overexpression and purification of bioactive human growth hormone by fusion to thioredoxin, maltose binding protein, and protein disulfide isomerase.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- Novel Anti-Mesothelin Nanobodies and Recombinant Immunotoxins withMolecules and cells · 2023Article
- Growth hormone receptor agonists and antagonists: From protein expression and purification to long-acting formulations.Protein science : a publication of the Protein Society · 2023Review
- Soluble Cytoplasmic Expression and Purification of Immunotoxin HER2(scFv)-PE24B as a Maltose Binding Protein Fusion.International journal of molecular sciences · 2021Article
- Novel Bacterial Production of Two Different Bioactive Forms of Human Stem-Cell Factor.International journal of molecular sciences · 2021Article
- Soluble Prokaryotic Overexpression and Purification of Human GM-CSF Using the Protein Disulfide Isomerase b'a' Domain.International journal of molecular sciences · 2021Article
- Engineered small metal-binding protein tag improves the production of recombinant human growth hormone in the periplasm of Escherichia coli.FEBS open bio · 2020Article
- Prokaryotic soluble overexpression and purification of oncostatin M using a fusion approach and genetically engineered E. coli strains.Scientific reports · 2019Article
- Molecular Characterization and Heterologous Production of the Bacteriocin Peocin, a DNA Starvation/Stationary Phase Protection Protein, fromMolecules (Basel, Switzerland) · 2019Article
- mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins inInternational journal of molecular sciences · 2019Article
- Bioprocess and downstream optimization of recombinant human growth hormone inResearch in pharmaceutical sciences · 2018Article
- Effect of Twine-arginine Translocation-signaling Fusion System and Chaperones Co-expression on Secretory Expression of Somatropin.Advanced biomedical research · 2018Article
- Prokaryotic soluble expression and purification of bioactive human fibroblast growth factor 21 using maltose-binding protein.Scientific reports · 2017Article
- Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase.The protein journal · 2017Article
- Twin arginine translocation system in secretory expression of recombinant human growth hormone.Research in pharmaceutical sciences · 2016Article
- Recombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tag.Microbial cell factories · 2016Article
- Prokaryotic Soluble Overexpression and Purification of Human VEGF165 by Fusion to a Maltose Binding Protein Tag.PloS one · 2016Article
- A Novel and Fast Purification Method for Nucleoside Transporters.Frontiers in molecular biosciences · 2016Article
- Article
- Use of Ubp1 protease analog to produce recombinant human growth hormone in Escherichia coli.Microbial cell factories · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human growth hormone (hGH) is synthesized by somatotroph cells of the anterior pituitary gland and induces cell proliferation and growth. This protein has been approved for the treatment of various conditions, including hGH deficiency, chronic renal failure, and Turner syndrome. Efficient production of hGH in Escherichia coli (E. coli) has proven difficult because the E. coli-expressed hormone tends to aggregate and form inclusion bodies, resulting in poor solubility. In this study, seven N-terminal fusion partners, hexahistidine (His6), thioredoxin (Trx), glutathione S-transferase (GST), maltose-binding protein (MBP), N-utilization substance protein A (NusA), protein disulfide bond isomerase (PDI), and the b'a' domain of PDI (PDIb'a'), were tested for soluble overexpression of codon-optimized hGH in E. coli. We found that MBP and hPDI tags significantly increased the solubility of the hormone. In addition, lowering the expression temperature to 18°C also dramatically increased the solubility of all the fusion proteins. We purified hGH from MBP-, PDIb'a'-, or Trx-tagged hGH expressed at 18°C in E. coli using simple chromatographic techniques and compared the final purity, yield, and activity of hGH to assess the impact of each partner protein. Purified hGH was highly pure on silver-stained gel and contained very low levels of endotoxin. On average, ∼37 mg, ∼12 mg, and ∼7 mg of hGH were obtained from 500 mL-cell cultures of Trx-hGH, MBP-hGH, and PDIb'a'-hGH, respectively. Subsequently, hGH was analyzed using mass spectroscopy to confirm the presence of two intra-molecular disulfide bonds. The bioactivity of purified hGHs was demonstrated using Nb2-11 cell.
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