Prothymosin alpha binds to histone H1 in vitro

dc.contributor.authorPapamarcaki, T.en
dc.contributor.authorTsolas, O.en
dc.date.accessioned2015-11-24T18:55:51Z
dc.date.available2015-11-24T18:55:51Z
dc.identifier.issn0014-5793-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18941
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectCattleen
dc.subjectCell-Free Systemen
dc.subjectHistones/*metabolismen
dc.subjectLigandsen
dc.subjectMolecular Sequence Dataen
dc.subjectProtein Bindingen
dc.subjectProtein Precursors/*metabolismen
dc.subjectSubcellular Fractions/metabolismen
dc.subjectThymosin/*analogs & derivatives/metabolismen
dc.subjectThymus Gland/metabolismen
dc.titleProthymosin alpha binds to histone H1 in vitroen
heal.abstractPrevious studies have shown that prothymosin alpha (ProT alpha) is a nuclear acidic protein implicated in cell proliferation. To identify proteins that interact with ProT alpha we have used ligand-blotting assays. We report here that purified ProT alpha binds specifically to histone H1 in a dose dependent manner. Polyglutamic acid, an analog of the central acidic domain of ProT alpha, strongly inhibits the above interaction, suggesting that the binding of ProT alpha to histone H1 is mediated through its acidic domain.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/8194604-
heal.identifier.secondaryhttp://ac.els-cdn.com/0014579394004390/1-s2.0-0014579394004390-main.pdf?_tid=81ec50e683095f19c309446c94a4a27e&acdnat=1337848948_125f4dac88673716d3854eebceaf5b66-
heal.journalNameFEBS Letten
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1994-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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