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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18886
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dc.contributor.authorLemuh, N. D.en
dc.contributor.authorDiallinas, G.en
dc.contributor.authorFrillingos, S.en
dc.contributor.authorMermelekas, G.en
dc.contributor.authorKaragouni, A. D.en
dc.contributor.authorHatzinikolaou, D. G.en
dc.date.accessioned2015-11-24T18:55:28Z-
dc.date.available2015-11-24T18:55:28Z-
dc.identifier.issn1096-0279-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18886-
dc.rightsDefault Licence-
dc.subjectAspergillus nidulans/*enzymologyen
dc.subjectChromatography, Affinityen
dc.subjectChromatography, Gelen
dc.subjectCircular Dichroismen
dc.subjectCloning, Molecularen
dc.subjectEthanol/metabolismen
dc.subject*Fungal Proteins/chemistry/genetics/isolation & purification/metabolismen
dc.subjectGlucose/metabolismen
dc.subjectImmunoblottingen
dc.subject*Membrane Transport Proteins/chemistry/genetics/isolation &en
dc.subjectpurification/metabolismen
dc.subjectPromoter Regions, Geneticen
dc.subjectRecombinant Fusion Proteins/chemistry/genetics/isolation &en
dc.subjectpurification/metabolismen
dc.subjectSpectrum Analysisen
dc.titlePurification and partial characterization of the xanthine-uric acid transporter (UapA) of Aspergillus nidulansen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1016/j.pep.2008.08.012-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/18824106-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1046592808002179/1-s2.0-S1046592808002179-main.pdf?_tid=da076eebdfe421ade6a7f73c399db862&acdnat=1332912871_6761c200c942af266d38509fb74fa6b5-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2009-
heal.abstractUapA, the uric acid-xanthine permease from the filamentous ascomycete Aspergillus nidulans, is one of the most thoroughly characterized purine/H(+) transporters in eukaryotes. Detailed studies have addressed its regulation of expression, at both the transcriptional and post-translational levels, in response to physiological and developmental signals. An extensive kinetic profile towards a plethora of purines and mutational analyses have established models on how UapA recognizes the purine ring and revealed specific amino acid residues involved in proper folding, topogenesis, function and specificity. The present work describes for the first time the purification of the UapA transporter of A. nidulans through overexpression via the strong, ethanol-inducible, glucose-repressible, alcA promoter. Purification, almost to homogeneity, was achieved by Ni(2+) affinity chromatography using a functional His-tagged UapA protein version. It is subsequently shown, by Circular Dichroism (CD) spectroscopy, that the purified protein is structured with a high alpha-helical content, as expected from the in silico predictions. The result of this work opens the way for further, analytical and biochemical studies on UapA at the protein level.en
heal.journalNameProtein Expr Purifen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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