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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/21772
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dc.contributor.authorPontremoli, S.en
dc.contributor.authorMelloni, E.en
dc.contributor.authorDe Flora, A.en
dc.contributor.authorAccorsi, A.en
dc.contributor.authorBalestrero, F.en
dc.contributor.authorTsolas, O.en
dc.contributor.authorHorecker, B. L.en
dc.contributor.authorPoole, B.en
dc.date.accessioned2015-11-24T19:17:23Z-
dc.date.available2015-11-24T19:17:23Z-
dc.identifier.issn0300-9084-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21772-
dc.rightsDefault Licence-
dc.subjectAcid Phosphatase/analysisen
dc.subjectAnimalsen
dc.subjectCatalase/analysisen
dc.subjectCathepsins/analysisen
dc.subjectCytoplasm/enzymologyen
dc.subjectElectron Transport Complex IV/analysisen
dc.subject*Fastingen
dc.subjectFemaleen
dc.subjectFructose-Bisphosphatase/*metabolismen
dc.subjectLiver/*enzymologyen
dc.subjectLysosomes/drug effects/*enzymologyen
dc.subjectMembranes/enzymologyen
dc.subjectOsmotic Fragilityen
dc.subjectPeptide Fragments/metabolismen
dc.subjectPeptide Hydrolases/*analysisen
dc.subjectPolyethylene Glycols/pharmacologyen
dc.subjectRabbitsen
dc.subjectRatsen
dc.titleEvidence for the selective release of lysosomal proteinases in fasted rabbitsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/182282-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0300908476803653/1-s2.0-S0300908476803653-main.pdf?_tid=f81cd65b4c9c7bb68db0b3e77d2b3a10&acdnat=1337849048_02d668035872312aa9df0b1e82d0ef07-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1976-
heal.abstractThe enzyme responsible for the conversion of "neutral" to "alkaline" fructose 1,6-bisphosphatase (EC 3.1.3.11) by removal of a 7000 dalton peptide (converting enzyme, Proteinase I) has been shown to be localized in rat liverlysosomes. Lysosomes also contain a specific proteinase (Proteinase II) that catalyzes the release of a small peptide from the NH2-terminus of the native subunits. In fasted rabbits Proteinase II is released into the cytoplasm, together with Cathepsin A, but Proteinase I remains associated with the lysosomal fraction. Increased osmotic fragility of liver lysosomes in fasted rabbits has also been observed, but this increased fragility does not result in the release of Proteinase I. The appearance of Proteinase II in the cytoplasm may be due either to its selective release from the lysosomes, without release of Proteinase I, or its localization in a different lysosomal fraction. Changes in lysosomal structure induced by fasting may play a dual role in : 1) the mobilization of amino acids for gluconeogenesis and 2) the modulation of activity of gluconeogenic enzymes.en
heal.journalNameBiochimieen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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