Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81778
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dc.contributor.authorJeong, Taeck-Hyunen
dc.contributor.authorSon, Young-Jinen
dc.contributor.authorRyu, Han-Bongen
dc.contributor.authorKoo, Bon-Kyungen
dc.contributor.authorJeong, Seung-Mien
dc.contributor.authorHoang, Phuongen
dc.contributor.authorDo, Bich Hangen
dc.contributor.authorSong, Jung-Aen
dc.contributor.authorChong, Seon-Haen
dc.contributor.authorRobinson, Robert Charlesen
dc.contributor.authorChoe, Hanen
dc.date.accessioned2016-07-20T05:16:55Zen
dc.date.accessioned2019-12-06T14:40:25Z-
dc.date.available2016-07-20T05:16:55Zen
dc.date.available2019-12-06T14:40:25Z-
dc.date.issued2014en
dc.identifier.citationJeong, T.-H., Son, Y.-J., Ryu, H.-B., Koo, B.-K., Jeong, S.-M., Hoang, P., et al. (2014). Soluble expression and partial purification of recombinant human erythropoietin from E. coli. Protein Expression and Purification, 95, 211-218.en
dc.identifier.issn1046-5928en
dc.identifier.urihttps://hdl.handle.net/10356/81778-
dc.identifier.urihttp://hdl.handle.net/10220/40978en
dc.description.abstractHuman erythropoietin (hEpo) is an essential regulator of erythrocyte production that induces the division and differentiation of erythroid progenitor cells in the bone marrow into mature erythrocytes. It is widely used for the treatment of anemia resulting from chronic kidney disease, chemotherapy, and cancer-related therapies. Active hEpo, and hEpo analogs, have been purified primarily from mammalian cells, which has several disadvantages, including low yields and high production costs. Although an Escherichia coli (E. coli) expression system may provide economic production of therapeutic proteins, it has not been used for the production of recombinant hEpo (rhEpo) because it aggregates in inclusion bodies in the E. coli cytoplasm and is not modified post-translationally. We investigated the soluble overexpression of active rhEpo with various protein tags in E. coli, and found out that several tags increased the solubility of rhEpo. Among them maltose binding protein (MBP)-tagged rhEpo was purified using affinity and gel filtration columns. Non-denaturing electrophoresis and MALDI-TOF MS analysis demonstrated that the purified rhEpo had two intra-disulfide bonds identical to those of the native hEpo. An in vitro proliferation assay showed that rhEpo purified from E. coli had similar biological activity as rhEpo derived from CHO cells. Therefore, we report for the first time that active rhEpo was overexpressed as a soluble form in the cytoplasm of E. coli and purified it in simple purification steps. We hope that our results offer opportunities for progress in rhEpo therapeutics.en
dc.description.sponsorshipASTAR (Agency for Sci., Tech. and Research, S’pore)en
dc.language.isoenen
dc.relation.ispartofseriesProtein Expression and Purificationen
dc.rights© 2014 Elsevier.en
dc.subjectrhEpoen
dc.subjectEscherichia coli expression systemen
dc.titleSoluble expression and partial purification of recombinant human erythropoietin from E. colien
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doihttp://dx.doi.org/10.1016/j.pep.2014.01.001en
item.grantfulltextnone-
item.fulltextNo Fulltext-
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