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E. coli 발현 시스템에 의해 생산된 recombinant human bone morphogenetic protein-2의 정제와 생물학적 활성
DC Field | Value | Language |
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dc.contributor.author | 조규성 | - |
dc.date.accessioned | 2015-05-19T16:54:28Z | - |
dc.date.available | 2015-05-19T16:54:28Z | - |
dc.date.issued | 2008 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/107164 | - |
dc.description.abstract | Purpose: 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.statementOfResponsibility | open | - |
dc.format | application/pdf | - |
dc.relation.isPartOf | Journal of Korean Academy of Periodontology (대한치주과학회지) | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | E. coli 발현 시스템에 의해 생산된 recombinant human bone morphogenetic protein-2의 정제와 생물학적 활성 | - |
dc.title.alternative | Purification and biological activity of recombinant human bone morphogenetic protein-2 produced by E. coli expression system | - |
dc.type | Article | - |
dc.contributor.college | College of Dentistry (치과대학) | - |
dc.contributor.department | Dept. of Periodontology (치주과학) | - |
dc.contributor.googleauthor | 최경희 | - |
dc.contributor.googleauthor | 문금옥 | - |
dc.contributor.googleauthor | 김수홍 | - |
dc.contributor.googleauthor | 윤정호 | - |
dc.contributor.googleauthor | 장경립 | - |
dc.contributor.googleauthor | 조규성 | - |
dc.identifier.doi | 10.5051/jkape.2008.38.1.41 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A03810 | - |
dc.relation.journalcode | J01492 | - |
dc.contributor.alternativeName | Cho, Kyoo Sung | - |
dc.contributor.affiliatedAuthor | Cho, Kyoo Sung | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 38 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 41 | - |
dc.citation.endPage | 50 | - |
dc.identifier.bibliographicCitation | Journal of Korean Academy of Periodontology (대한치주과학회지), Vol.38(1) : 41-50, 2008 | - |
dc.identifier.rimsid | 46032 | - |
dc.type.rims | ART | - |
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