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dc.contributor.authorGueorguieva, Ludmila
dc.contributor.authorVallejo, Luis Felipe
dc.contributor.authorRinas, Ursula
dc.contributor.authorSeidel-Morgenstern, Andreas
dc.date.accessioned2008-01-08T15:15:34Z
dc.date.available2008-01-08T15:15:34Z
dc.date.issued2006-12-01
dc.identifier.citationDiscontinuous and continuous separation of the monomeric and dimeric forms of human bone morphogenetic protein-2 from renaturation batches. 2006, 1135 (2):142-50notJ Chromatogr Aen
dc.identifier.issn0021-9673
dc.identifier.pmid17064713
dc.identifier.doi10.1016/j.chroma.2006.08.061
dc.identifier.urihttp://hdl.handle.net/10033/15836
dc.description.abstractBone morphogenetic protein-2 (BMP-2) is one of the most interesting of the approximately 14 BMPs which belong to the transforming-growth-factor-beta (TGF-beta) superfamily. BMP-2 induces bone formation and thus plays an important role as a pharmaceutical protein. Recently, rhBMP-2 has been produced in form of inactive inclusion bodies in Escherichia coli. After solubilization and renaturation the biologically active dimeric form of rhBMP-2 can be generated. However, inactive monomers of BMP-2 are also formed during the renaturation process which must be separated from the active dimeric BMP-2. The purpose of this paper is to present: (a) results of an experimental study of a chromatographic separation of the monomeric and dimeric forms; and (b) a concept for a continuous counter-current simulated moving bed (SMB) process. The capacity of heparin as stationary phase was estimated for different salt concentrations in the mobile phase. A simulation study of a three-zone SMB process was performed applying a two step salt gradient. The results reveal the potential of the process for the purification of the dimeric BMP-2.
dc.language.isoenen
dc.subject.meshBone Morphogenetic Proteinsen
dc.subject.meshChromatography, Liquiden
dc.subject.meshDimerizationen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshEscherichia colien
dc.subject.meshHeparinen
dc.subject.meshProtein Renaturationen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshSpectrophotometry, Ultravioleten
dc.subject.meshTransforming Growth Factor betaen
dc.titleDiscontinuous and continuous separation of the monomeric and dimeric forms of human bone morphogenetic protein-2 from renaturation batches.en
dc.typeArticleen
dc.contributor.departmentOtto-von-Guericke-Universität Magdeburg, Institut für Verfahrenstechnik, PO Box 4120, D-39106 Magdeburg, Germany.en
dc.identifier.journalJournal of chromatography. Aen
refterms.dateFOA2018-06-12T16:47:54Z
html.description.abstractBone morphogenetic protein-2 (BMP-2) is one of the most interesting of the approximately 14 BMPs which belong to the transforming-growth-factor-beta (TGF-beta) superfamily. BMP-2 induces bone formation and thus plays an important role as a pharmaceutical protein. Recently, rhBMP-2 has been produced in form of inactive inclusion bodies in Escherichia coli. After solubilization and renaturation the biologically active dimeric form of rhBMP-2 can be generated. However, inactive monomers of BMP-2 are also formed during the renaturation process which must be separated from the active dimeric BMP-2. The purpose of this paper is to present: (a) results of an experimental study of a chromatographic separation of the monomeric and dimeric forms; and (b) a concept for a continuous counter-current simulated moving bed (SMB) process. The capacity of heparin as stationary phase was estimated for different salt concentrations in the mobile phase. A simulation study of a three-zone SMB process was performed applying a two step salt gradient. The results reveal the potential of the process for the purification of the dimeric BMP-2.


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