Purification and characterization of recombinant human erythropoietin from milk of transgenic pigs

Cited 4 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorEun Gyo Lee-
dc.contributor.authorSeung-hui Lee-
dc.contributor.authorKyung Mi Park-
dc.contributor.authorJ E Baek-
dc.contributor.authorSeon Hee Yeon-
dc.contributor.authorJ K Park-
dc.contributor.authorW K Chang-
dc.contributor.authorJoon Ki Jung-
dc.contributor.authorBong Hyun Chung-
dc.date.accessioned2017-04-19T09:13:41Z-
dc.date.available2017-04-19T09:13:41Z-
dc.date.issued2009-
dc.identifier.issn02682575-
dc.identifier.uri10.1002/jctb.2094ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8930-
dc.description.abstractBACKGROUND: Human erythropoietin (hEPO), a hydrophobic acidic glycoprotein responsible for the regulation of red blood cell production in mammals, is used for the treatment of anemia. In general, the purification of transgenic animal-derived therapeutic proteins is not easy due to their low titer concentrations and abundant contaminant proteins. For the first time, here the purification and characterization of rhEPO from themilk of transgenic pigs are described. RESULTS: The rhEPO was purified by heparin chromatography, reverse-phase chromatography, and gel filtration chromatography, resulting in a 16.5% yield and >98% purity. The rhEPO purified from the milk of transgenic pigs contained less acidic isoforms andwas underglycosylated in contrast to CHO-derived rhEPO. Cell proliferation of the F-36/EPO-dependent cell line was proportional to the dose of transgenic pig-derived rhEPO. CONCLUSION:Transgenicpig-derivedrhEPOwithhighpuritywas achieved after three-step chromatographyfollowing two-step precipitation. The transgenic pig-derived rhEPO was demonstrated to have comparable potency with CHO-derived rhEPO. Transgenic pig-derived rhEPO may not be therapeutically feasible because of different glycosylation, and thus further studies are required to elucidate the effect of this aberrant glycosylation on the biological activity and stability in vivo.-
dc.publisherWiley-
dc.titlePurification and characterization of recombinant human erythropoietin from milk of transgenic pigs-
dc.title.alternativePurification and characterization of recombinant human erythropoietin from milk of transgenic pigs-
dc.typeArticle-
dc.citation.titleJournal of Chemical Technology and Biotechnology-
dc.citation.number5-
dc.citation.endPage649-
dc.citation.startPage643-
dc.citation.volume84-
dc.contributor.affiliatedAuthorEun Gyo Lee-
dc.contributor.alternativeName이은교-
dc.contributor.alternativeName이승희-
dc.contributor.alternativeName박경미-
dc.contributor.alternativeName백정은-
dc.contributor.alternativeName연선희-
dc.contributor.alternativeName박진기-
dc.contributor.alternativeName장원경-
dc.contributor.alternativeName정준기-
dc.contributor.alternativeName정봉현-
dc.identifier.bibliographicCitationJournal of Chemical Technology and Biotechnology, vol. 84, no. 5, pp. 643-649-
dc.identifier.doi10.1002/jctb.2094-
dc.subject.keywordtransgenic pig-
dc.subject.keywordrecombinant human erythropoietin(rhEPO)-
dc.subject.keywordpurification-
dc.subject.keywordglycosylation-
dc.subject.localtransgenic pig-
dc.subject.localTransgenic pig-
dc.subject.localrecombinant human erythropoietin(rhEPO)-
dc.subject.localpurification-
dc.subject.localPurification-
dc.subject.localglycosylation-
dc.subject.localGlycosylation-
dc.description.journalClassY-
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.