{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T09:09:22Z","timestamp":1768208962350,"version":"3.49.0"},"reference-count":54,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2014,3,10]],"date-time":"2014-03-10T00:00:00Z","timestamp":1394409600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0089038","type":"journal-article","created":{"date-parts":[[2014,3,10]],"date-time":"2014-03-10T20:32:56Z","timestamp":1394483576000},"page":"e89038","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":39,"title":["Prokaryotic Soluble Overexpression and Purification of Bioactive Human Growth Hormone by Fusion to Thioredoxin, Maltose Binding Protein, and Protein Disulfide Isomerase"],"prefix":"10.1371","volume":"9","author":[{"given":"Minh Tan","family":"Nguyen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bon-Kyung","family":"Koo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thu Trang","family":"Thi Vu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jung-A","family":"Song","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seon-Ha","family":"Chong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Boram","family":"Jeong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Han-Bong","family":"Ryu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sang-Hyun","family":"Moh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Han","family":"Choe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2014,3,10]]},"reference":[{"key":"ref1","first-page":"125","article-title":"Crosstalk between growth hormone and insulin signaling","volume":"80","author":"J Xu","year":"2009","journal-title":"VitamHorm"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1210\/edrv.22.1.0419","article-title":"The somatomedin hypothesis: 2001","volume":"22","author":"D Le Roith","year":"2001","journal-title":"Endocr Rev"},{"key":"ref3","first-page":"E261","article-title":"Effect of growth hormone and resistance exercise on muscle growth in young men","volume":"262","author":"KE Yarasheski","year":"1992","journal-title":"Am J Physiol"},{"key":"ref4","first-page":"S150","article-title":"Hormonal regulation of longitudinal bone growth","volume":"48 Suppl 1","author":"A Nilsson","year":"1994","journal-title":"Eur J ClinNutr"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1023\/A:1017941625858","article-title":"Growth hormone signalling and apoptosis in neonatal rat cardiomyocytes","volume":"223","author":"Y Gu","year":"2001","journal-title":"Mol Cell Biochem"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0303-7207(02)00014-X","article-title":"Growth hormone can act as a cytokine controlling survival and proliferation of immune cells: new insights into signaling pathways","volume":"188","author":"S Jeay","year":"2002","journal-title":"Mol Cell Endocrinol"},{"key":"ref7","first-page":"103","article-title":"History and future of growth hormone research","volume":"60 Suppl 3","author":"JJ Kopchick","year":"2003","journal-title":"Horm Res"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"S162","DOI":"10.4103\/2230-8210.84852","article-title":"History of growth hormone therapy","volume":"15 Suppl 3","author":"VS Ayyar","year":"2011","journal-title":"Indian J EndocrinolMetab"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/S0002-9343(98)00135-1","article-title":"Recombinant human growth hormone: old and novel uses","volume":"105","author":"NA Tritos","year":"1998","journal-title":"Am J Med"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1210\/jc.2007-1723","article-title":"Long-term safety of recombinant human growth hormone in turner syndrome","volume":"93","author":"K Bolar","year":"2008","journal-title":"J ClinEndocrinolMetab"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.ecl.2009.06.006","article-title":"Growth hormone: the expansion of available products and indications","volume":"38","author":"SL Franklin","year":"2009","journal-title":"EndocrinolMetabClin North Am"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1126\/science.377496","article-title":"Human growth hormone: complementary DNA cloning and expression in bacteria","volume":"205","author":"JA Martial","year":"1979","journal-title":"Science"},{"key":"ref13","first-page":"126","article-title":"Purification of recombinant human growth hormone from CHO cell culture supernatant by Gradiflow preparative electrophoresis technology","volume":"32","author":"D Catzel","year":"2003","journal-title":"Protein ExprPurif"},{"key":"ref14","first-page":"221","article-title":"Expression system for synthesis and purification of recombinant human growth hormone in Pichiapastoris and structural analysis by MALDI-ToF Mass Spectrometry","volume":"24","author":"P Calik","year":"2008","journal-title":"BiotechnolProg"},{"key":"ref15","first-page":"197","article-title":"Efficient expression and secretion of recombinant human growth hormone in the methylotrophic yeast Pichiapastoris: potential applications for other proteins","volume":"54","author":"A Apte-Deshpande","year":"2009","journal-title":"BiotechnolApplBiochem"},{"key":"ref16","first-page":"306462","article-title":"In vivo bioassay of recombinant human growth hormone synthesized in B. mori pupae","volume":"2010","author":"H Lan","year":"2010","journal-title":"J Biomed Biotechnol"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0168-1656(98)00054-6","article-title":"High-level production of human growth hormone in Escherichia coli by a simple recombinant process","volume":"62","author":"NK Shin","year":"1998","journal-title":"Journal of Biotechnology"},{"key":"ref18","first-page":"182","article-title":"Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli","volume":"18","author":"AK Patra","year":"2000","journal-title":"Protein ExprPurif"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.ghir.2006.07.002","article-title":"Large-scale preparation and in vitro characterization of biologically active human placental (20 and 22K) and pituitary (20K) growth hormones: placental growth hormones have no lactogenic activity in humans","volume":"16","author":"G Solomon","year":"2006","journal-title":"Growth Hormone and IGF Research"},{"key":"ref20","first-page":"2675","article-title":"Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia coli","volume":"72","author":"H Sonoda","year":"2008","journal-title":"BiosciBiotechnolBiochem"},{"key":"ref21","first-page":"54","article-title":"High throughput purification of recombinant human growth hormone using radial flow chromatography","volume":"68","author":"SM Singh","year":"2009","journal-title":"Protein ExprPurif"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/b93995","article-title":"Inclusion bodies: formation and utilisation","volume":"89","author":"B Fahnert","year":"2004","journal-title":"Advances in Biochemical Engineering\/Biotechnology"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0014-5793(86)81403-X","article-title":"Expression, secretion and folding of human growth hormone in Escherichia coli. Purification and characterization","volume":"204","author":"GW Becker","year":"1986","journal-title":"FEBS Letters"},{"key":"ref24","first-page":"129","article-title":"Periplasmic production via the pET expression system of soluble, bioactive human growth hormone","volume":"87","author":"JT Sockolosky","year":"2013","journal-title":"Protein ExprPurif"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"e56168","DOI":"10.1371\/journal.pone.0056168","article-title":"Complete solubilization and purification of recombinant human growth hormone produced in Escherichia coli","volume":"8","author":"MJ Kim","year":"2013","journal-title":"PLoS One"},{"key":"ref26","first-page":"579","article-title":"Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate","volume":"17","author":"TY Koo","year":"2007","journal-title":"J MicrobiolBiotechnol"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1007\/s00253-012-4553-7","article-title":"Rational and efficient preparation of a chimeric protein containing a tandem dimer of thrombopoietin mimetic peptide fused to human growth hormone in Escherichia coli","volume":"97","author":"S Wang","year":"2013","journal-title":"Applied Microbiology and Biotechnology"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"1788","DOI":"10.1101\/gr.143000","article-title":"DNA cloning using in vitro site-specific recombination","volume":"10","author":"JL Hartley","year":"2000","journal-title":"Genome Res"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/j.ab.2005.05.015","article-title":"Construction of a set Gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli","volume":"343","author":"D Busso","year":"2005","journal-title":"Analytical Biochemistry"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/s12010-013-0140-3","article-title":"Expression and purification of biologically active human FGF2 containing the b\u2032a\u2032 domains of human PDI in <italic>Escherichia coli<\/italic>","volume":"170","author":"JA Song","year":"2013","journal-title":"Applied Biochemistry and Biotechnology"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"MM Bradford","year":"1976","journal-title":"Anal Biochem"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1093\/protein\/14.12.993","article-title":"Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency","volume":"14","author":"RB Kapust","year":"2001","journal-title":"Protein Engineering"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/nature04537","article-title":"The PerR transcription factor senses H2O2 by metal-catalysedhistidine oxidation","volume":"440","author":"JW Lee","year":"2006","journal-title":"Nature"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"e83781","DOI":"10.1371\/journal.pone.0083781","article-title":"Soluble Expression of Human Leukemia Inhibitory Factor with Protein Disulfide Isomerase in Escherichia coli and Its Simple Purification","volume":"8","author":"AS Jung","year":"2013","journal-title":"PLoS One"},{"key":"ref35","first-page":"283","article-title":"An overview of enzymatic reagents for the removal of affinity tags","volume":"80","author":"DS Waugh","year":"2011","journal-title":"Protein ExprPurif"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1210\/jcem-51-5-1058","article-title":"A new sensitive and specific bioassay for lactogenic hormones: measurement of prolactin and growth hormone in human serum","volume":"51","author":"T Tanaka","year":"1980","journal-title":"J ClinEndocrinolMetab"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0006-8993(90)90651-Q","article-title":"The distribution of lactogen receptors in the mammalian hypothalamus: an in vitro autoradiographic analysis of the rabbit and rat","volume":"530","author":"RJ Walsh","year":"1990","journal-title":"Brain Res"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev.bi.54.070185.001321","article-title":"Thioredoxin","volume":"54","author":"A Holmgren","year":"1985","journal-title":"Annu Rev Biochem"},{"key":"ref39","first-page":"1287","article-title":"Reactive oxygen species, antioxidants, and the mammalian thioredoxin system","volume":"31","author":"J Nordberg","year":"2001","journal-title":"Free RadicBiol Med"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1006\/jmbi.2001.4914","article-title":"Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies","volume":"312","author":"H Bach","year":"2001","journal-title":"Journal of Molecular Biology"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1110\/ps.8.8.1668","article-title":"Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused","volume":"8","author":"RB Kapust","year":"1999","journal-title":"Protein Science"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1016\/j.jmb.2007.02.091","article-title":"Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis","volume":"368","author":"C Park","year":"2007","journal-title":"J MolBiol"},{"key":"ref43","first-page":"35","article-title":"Protein disulfide isomerase","volume":"1699","author":"B Wilkinson","year":"2004","journal-title":"BiochimBiophysActa"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nmeth.f.202","article-title":"Protein production and purification","volume":"5","author":"S Graslund","year":"2008","journal-title":"Nat Methods"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1016\/S0006-3495(96)79404-3","article-title":"How Hofmeister ion interactions affect protein stability","volume":"71","author":"RL Baldwin","year":"1996","journal-title":"Biophys J"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0022-2836(02)00137-7","article-title":"NMR studies of the backbone flexibility and structure of human growth hormone: a comparison of high and low pH conformations","volume":"318","author":"MR Kasimova","year":"2002","journal-title":"J MolBiol"},{"key":"ref47","first-page":"67","article-title":"Growth hormone isoforms and segments\/fragments: molecular structure and laboratory measurement","volume":"364","author":"EF De Palo","year":"2006","journal-title":"ClinChimActa"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1126\/science.154.3750.785","article-title":"Retention of the biological potency of human pituitary growth hormone after reduction and carbamidomethylation","volume":"154","author":"JS Dixon","year":"1966","journal-title":"Science"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1210\/jcem-37-4-499","article-title":"Retention of biologic activity of human growth hormone in man after reduction and alkylation","volume":"37","author":"MH Connors","year":"1973","journal-title":"J ClinEndocrinolMetab"},{"key":"ref50","first-page":"312","article-title":"Conserved and unique amino acid residues in the domains of the growth hormones. Flounder growth hormone deduced from the cDNA sequence has the minimal size in the growth hormone prolactin gene family","volume":"264","author":"M Watahiki","year":"1989","journal-title":"J BiolChem"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.2471267","article-title":"High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis","volume":"244","author":"BC Cunningham","year":"1989","journal-title":"Science"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"2493","DOI":"10.1210\/jc.2004-1838","article-title":"Short stature caused by a biologically inactive mutant growth hormone (GH-C53S)","volume":"90","author":"A Besson","year":"2005","journal-title":"J ClinEndocrinolMetab"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"300","DOI":"10.5603\/EP.2013.0009","article-title":"Significance of the disulphide bonds of human growth hormone","volume":"64","author":"RK Junnila","year":"2013","journal-title":"Endokrynol Pol"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.ghir.2009.04.011","article-title":"Growth hormone isoforms","volume":"19","author":"GP Baumann","year":"2009","journal-title":"Growth Horm IGF Res"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0089038","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,24]],"date-time":"2018-10-24T02:36:11Z","timestamp":1540348571000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0089038"}},"subtitle":[],"editor":[{"given":"Sue","family":"Cotterill","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2014,3,10]]},"references-count":54,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2014,3,10]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0089038","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,3,10]]}}}