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E. coli 발현 시스템에 의해 생산된 recombinant human bone morphogenetic protein-2의 정제와 생물학적 활성

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dc.contributor.author조규성-
dc.date.accessioned2015-05-19T16:54:28Z-
dc.date.available2015-05-19T16:54:28Z-
dc.date.issued2008-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/107164-
dc.description.abstractPurpose: Bone morphogenetic protein-2(BMP-2) has been shown to possess significant osteoinducitve potential. There have been attempts to overcome a limitation of mass production, and economical efficiency of BMP. The aim of this study was to produce recombinant human BMP-2(rhBMP-2) from E. coli in a large scale and evaluate its biological activity. Materials and Methods: The E.coli strain BL21(DE3) was used as a host for rhBMP-2 production. Dimerized rhBMP-2 was purified by affinity chromatography using Heparin column. To determine the physicochemical properties of the rhBMP-2 expressed in E. coli, we examined the HPLC profile and performed Western blot analysis. The effect of the purified rhBMP-2 dimer on osteoblast differentiation was examined by alkaline phosphatase (ALP) activity and representing morphological change using C2C12 cell. Results: E. coli was genetically engineered to produce rhBMP-2 in a non-active aggregated form. We have established a method which involves refolding and purifying a folded rhBMP-2 dimer from non-active aggregates. The purified rhBMP-2 homodimer was characterized by SDS-PAGE as molecular weight of about 28kDa and eluted at 34% acetonitrile, 13.27 min(retention time) in the HPLC profile and detected at Western blot. The purified rhBMP-2 dimer stimulated ALP activity and induced the transformation from myogenic differentiation to osteogenic differentiation. Conclusion: rhBMP-2 was produced in E. coli using genetic engineering. The purified rhBMP-2 dimer stimulated ALP activity and induced the osteogenic differentiation of C2C12 cells.-
dc.description.statementOfResponsibilityopen-
dc.formatapplication/pdf-
dc.relation.isPartOfJournal of Korean Academy of Periodontology (대한치주과학회지)-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleE. coli 발현 시스템에 의해 생산된 recombinant human bone morphogenetic protein-2의 정제와 생물학적 활성-
dc.title.alternativePurification and biological activity of recombinant human bone morphogenetic protein-2 produced by E. coli expression system-
dc.typeArticle-
dc.contributor.collegeCollege of Dentistry (치과대학)-
dc.contributor.departmentDept. of Periodontology (치주과학)-
dc.contributor.googleauthor최경희-
dc.contributor.googleauthor문금옥-
dc.contributor.googleauthor김수홍-
dc.contributor.googleauthor윤정호-
dc.contributor.googleauthor장경립-
dc.contributor.googleauthor조규성-
dc.identifier.doi10.5051/jkape.2008.38.1.41-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA03810-
dc.relation.journalcodeJ01492-
dc.contributor.alternativeNameCho, Kyoo Sung-
dc.contributor.affiliatedAuthorCho, Kyoo Sung-
dc.rights.accessRightsfree-
dc.citation.volume38-
dc.citation.number1-
dc.citation.startPage41-
dc.citation.endPage50-
dc.identifier.bibliographicCitationJournal of Korean Academy of Periodontology (대한치주과학회지), Vol.38(1) : 41-50, 2008-
dc.identifier.rimsid46032-
dc.type.rimsART-
Appears in Collections:
2. College of Dentistry (치과대학) > Dept. of Periodontics (치주과학교실) > 1. Journal Papers

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