Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/30901
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dc.contributor.authorMaestro García-Donas, Beatriz-
dc.contributor.authorVelasco, Isabel-
dc.contributor.authorCastillejo, Isabel-
dc.contributor.authorArévalo-Rodríguez, Miguel-
dc.contributor.authorCebolla, Ángel-
dc.contributor.authorSanz, Jesús M-
dc.date.accessioned2024-01-31T13:50:32Z-
dc.date.available2024-01-31T13:50:32Z-
dc.date.created2008-
dc.identifier.citationJournal of Chromatography A . 2008 Oct 24;1208(1-2):189-96es_ES
dc.identifier.issn1873-3778-
dc.identifier.issn0021-9673-
dc.identifier.urihttps://hdl.handle.net/11000/30901-
dc.description.abstractWe present a novel procedure for affinity partitioning of recombinant proteins fused to the cholinebinding module C-LytA in aqueous two-phase systems containing poly(ethylene glycol) (PEG). Proteins tagged with the C-LytA module and exposed to the two-phase systems are quantitatively localized in the PEG-rich phase, whereas subsequent addition of the natural ligand choline specifically shifts their localization to the PEG-poor phase by displacement of the polymer from the binding sites. The described procedure is simple, scalable and reproducible, and has been successfully applied to the purification of four diverse proteins, resulting in high yields and purity.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent8es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsinfo:eu-repo/semantics/closedAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectAqueous two-phase systemses_ES
dc.subjectProtein purificationes_ES
dc.subjectPoly(ethylene glycol)es_ES
dc.subjectCholine-binding modulees_ES
dc.subjectLiquid–liquid extractiones_ES
dc.titleAffinity partitioning of proteins tagged with choline-binding modules in aqueous two-phase systemses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.contributor.instituteInstitutos de la UMH::Instituto de Bioingenieríaes_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.chroma.2008.08.106es_ES
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