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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/7473
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dc.contributor.authorGounaris, A.en
dc.contributor.authorTrangas, T. T.en
dc.contributor.authorTsiapalis, C. M.en
dc.date.accessioned2015-11-24T16:31:42Z-
dc.date.available2015-11-24T16:31:42Z-
dc.identifier.issn0003-9861-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7473-
dc.rightsDefault Licence-
dc.subjectAdenosine Triphosphate/metabolismen
dc.subjectChromatography, Gelen
dc.subjectCyclic AMP/*metabolismen
dc.subjectGuanosine Triphosphate/metabolismen
dc.subjectHumansen
dc.subjectIsoelectric Pointen
dc.subjectKineticsen
dc.subjectMolecular Weighten
dc.subjectProtein Kinases/*metabolismen
dc.subjectSpleen/*enzymologyen
dc.subjectSubstrate Specificityen
dc.titleSoluble cAMP-independent protein kinase from human spleenen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/2827577-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate1987-
heal.abstractA protein kinase (EC 2.7.1.37) was purified 2000-fold, from the soluble protein fraction of human spleen cells, using ion-exchange chromatography, ammonium sulfate fractionation, and gel filtration. This rapid procedure yielded 30% of the initial activity and an enzyme preparation with specific activity of 62 nmol min-1 mg-1 of protein. On the basis of disc gel electrophoresis in sodium dodecyl sulfate acrylamide gels and isoelectric focusing the enzyme preparation appears homogeneous and to consist of one polypeptide with a molecular weight of 43,000 and having a pI of 7.1. The purified enzyme activity is cyclic AMP and cGMP independent phosphorylates both alpha-casein and phosvitin, and uses Mg2+ ATP and Mg2+ GTP as phosphate donors, exhibiting an apparent Km of 2.0 and 6.6 X 10(-5)m, respectively. Furthermore, the enzyme activity is strongly inhibited by heparin (K50 = 0.1 micrograms/ml). These catalytic properties are characteristic of the enzyme casein kinase II, as described in several eukaryotic cells.en
heal.journalNameArch Biochem Biophysen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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