Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/22589
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dc.contributor.authorPapamarcaki, T.en
dc.contributor.authorTsolas, O.en
dc.date.accessioned2015-11-24T19:25:13Z-
dc.date.available2015-11-24T19:25:13Z-
dc.identifier.issn0014-4754-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/22589-
dc.rightsDefault Licence-
dc.subjectBlotting, Westernen
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectFemaleen
dc.subjectFructose-Bisphosphatase/isolation & purification/*metabolismen
dc.subjectHumansen
dc.subjectHydrogen-Ion Concentrationen
dc.subjectKineticsen
dc.subjectMacromolecular Substancesen
dc.subjectMolecular Weighten
dc.subjectPlacenta/*enzymologyen
dc.subjectPregnancyen
dc.titleDemonstration of fructose 1,6-bisphosphatase in human term placentaen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/1847882-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1991-
heal.abstractA proteolysed form of fructose 1,6-bisphosphatase (Fru-P2ase) has been detected and characterized in human term placenta. The extract was found to contain very low levels of activity with an alkaline pH optimum. Western blotting demonstrated a polypeptide of Mr 26,000, instead of the subunit of Mr 36,000 observed in native mammalian Fru-P2ases.en
heal.journalNameExperientiaen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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