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dc.contributor.authorCarratalá, Jose Vicente
dc.contributor.authorGifre-Renom, Laia
dc.contributor.authorRoca-Pinilla, Ramon
dc.contributor.authorVillaverde, Antonio
dc.contributor.authorArís, Anna
dc.contributor.authorGarcia-Fruitós, Elena
dc.contributor.authorSánchez, Julieta María
dc.contributor.authorFerrer-Miralles, Neus
dc.contributor.otherProducció Animalca
dc.date.accessioned2021-04-14T13:51:13Z
dc.date.available2021-04-14T13:51:13Z
dc.date.issued2021-03-16
dc.identifier.citationCarratalá, Jose Vicente, Laia Gifre-Renom, Ramon Roca-Pinilla, Antonio Villaverde, Anna Arís, Elena Garcia-Fruitós, Julieta María Sánchez, and Neus Ferrer-Miralles. 2021. "Selecting Subpopulations Of High-Quality Protein Conformers Among Conformational Mixtures Of Recombinant Bovine MMP-9 Solubilized From Inclusion Bodies". International Journal Of Molecular Sciences 22 (6): 3020. doi:10.3390/ijms22063020.ca
dc.identifier.issn1661-6596ca
dc.identifier.urihttp://hdl.handle.net/20.500.12327/1240
dc.description.abstractA detailed workflow to analyze the physicochemical characteristics of mammalian matrix metalloproteinase (MMP-9) protein species obtained from protein aggregates (inclusion bodies—IBs) was followed. MMP-9 was recombinantly produced in the prokaryotic microbial cell factories Clearcoli (an engineered form of Escherichia coli) and Lactococcus lactis, mainly forming part of IBs and partially recovered under non-denaturing conditions. After the purification by affinity chromatography of solubilized MMP-9, four protein peaks were obtained. However, so far, the different conformational protein species forming part of IBs have not been isolated and characterized. Therefore, with the aim to link the physicochemical characteristics of the isolated peaks with their biological activity, we set up a methodological approach that included dynamic light scattering (DLS), circular dichroism (CD), and spectrofluorometric analysis confirming the separation of subpopulations of conformers with specific characteristics. In protein purification procedures, the detailed analysis of the individual physicochemical properties and the biological activity of protein peaks separated by chromatographic techniques is a reliable source of information to select the best-fitted protein populations.ca
dc.format.extent15ca
dc.language.isoengca
dc.publisherMDPIca
dc.relation.ispartofInternational Journal of Molecular Sciencesca
dc.rightsAttribution 4.0 Internationalca
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleSelecting Subpopulations of High-Quality Protein Conformers among Conformational Mixtures of Recombinant Bovine MMP-9 Solubilized from Inclusion Bodiesca
dc.typeinfo:eu-repo/semantics/articleca
dc.description.versioninfo:eu-repo/semantics/publishedVersionca
dc.rights.accessLevelinfo:eu-repo/semantics/openAccess
dc.embargo.termscapca
dc.relation.projectIDMINECO/Programa Estatal de I+D+I orientada a los retos de la sociedad/AGL2015-00064-C02-01/ES/Validación del uso de las proteínas M-SAA3 y MMP-9 en la mejora del secado de la vaca de leche y optimización de su dosis efectiva mediante su nanoestructuración/ca
dc.relation.projectIDMINECO/Programa Estatal de I+D+I orientada a los retos de la sociedad/RTA2015-00064-C02-02/ES/Validación del uso de las proteínas M-SAA3 y MMP-9 en la mejora del secado de la vaca de leche y optimización de su dosis efectiva mediante su nanoestructuración/ca
dc.subject.udc619ca
dc.identifier.doihttps://doi.org/10.3390/ijms22063020ca
dc.contributor.groupProducció de Remugantsca


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