Light microscopic visualization of monoamine oxidase using a cerium method

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dc.contributor.authorNakos, G.en
dc.contributor.authorGossrau, R.en
dc.date.accessioned2015-11-24T19:07:16Z
dc.date.available2015-11-24T19:07:16Z
dc.identifier.issn0065-1281-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20417
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectCallithrixen
dc.subjectCerium/*chemistryen
dc.subjectFemaleen
dc.subjectGerbillinaeen
dc.subjectGuinea Pigsen
dc.subjectHistocytochemistryen
dc.subjectHumansen
dc.subject*Hydroxidesen
dc.subjectMaleen
dc.subjectMiceen
dc.subjectMice, Inbred Strainsen
dc.subjectMicroscopy/methodsen
dc.subjectMonoamine Oxidase/analysis/*metabolismen
dc.subjectMonoamine Oxidase Inhibitors/pharmacologyen
dc.subjectNervous System/enzymologyen
dc.subjectPeroxides/*chemistryen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.subjectSpecies Specificityen
dc.subjectTissue Distributionen
dc.titleLight microscopic visualization of monoamine oxidase using a cerium methoden
heal.abstractH2O2-generating monoamine oxidase can be visualized in the light microscope with tetrazolium, metal salt (ferricyanide) and coupled peroxidatic oxidation methods. Due to methodological draw-backs these procedures do no allow satisfactory results. In search for an alternative method a light microscopic cerium procedure was designed in which the primary reaction product, cerium perhydroxide, serves for the generation of amplified and intensified diaminobenzidine brown. With this cerium-diaminobenzidine-H2O2-Co method monoamine oxidase was visualized more easily and reliably and with higher sensitivity and more precise localization than with the other techniques. At present this method is considered to be the procedure of choice and was used to re-investigate and investigate the distribution of monoamine oxidase in rats, mice, gerbils, guinea-pigs, marmosets, monkeys and man. In these species many cells and tissues showed monoamine oxidase activity where the enzyme has not yet been found before and the structures with already known monoamine oxidase activity showed an improved localization.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/8135091-
heal.journalNameActa Histochemen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1993-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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