Light microscopic visualization of semicarbazide-sensitive amine oxidase (benzylamine oxidase) using a cerium method

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.issn0239-8508-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20416
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectBenzylamine Oxidase/analysis/*physiologyen
dc.subjectCallithrixen
dc.subjectCell Membrane/enzymology/metabolism/ultrastructureen
dc.subject*Ceriumen
dc.subjectFemaleen
dc.subjectGerbillinaeen
dc.subjectGuinea Pigsen
dc.subjectHistocytochemistry/*methodsen
dc.subjectHumansen
dc.subjectHydrogen Peroxide/metabolismen
dc.subjectMaleen
dc.subjectMiceen
dc.subjectMuscle, Smooth/cytology/enzymology/ultrastructureen
dc.subjectPlacenta/cytology/enzymology/ultrastructureen
dc.subjectPregnancyen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.subjectSemicarbazides/*pharmacologyen
dc.titleLight microscopic visualization of semicarbazide-sensitive amine oxidase (benzylamine oxidase) using a cerium methoden
heal.abstractLight microscopic histochemical studies to visualize semicarbazide-sensitive and H2O2-generating amine oxidase (SSAOX, benzylamine oxidase, BAOX; EC 1.4.3.6?) are usually performed with the coupled peroxidatic oxidation technique of Ryder et al. [25]. For methodological reasons this procedure has its limitations and was therefore replaced by a more reliable and easier to perform cerium-DAB-H2O2-Co technique. With this method SSAOX was studied in many organs of various laboratory rodents and marmosets and in human placenta. Independent of the species the enzyme was present mostly in the plasma membrane of nearly all vascular and non-vascular smooth muscle cells. However, there was a species-dependence of SSOX activity; the highest amounts of stain were found in gerbils and marmosets. In addition, the enzyme was found in these two species in the capillary endothelium of some extra-nervous tissues. The plasma membrane localization of SSAOX and plasma membrane-associated H2O2 production suggest a functional role for the enzyme different from that of other amine oxidases which appear to be primarily involved in intracellular amine detoxification or degradation.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/8026600-
heal.journalNameFolia Histochem Cytobiolen
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

Αρχεία

Φάκελος/Πακέτο αδειών

Προβολή: 1 - 1 of 1
Φόρτωση...
Μικρογραφία εικόνας
Ονομα:
license.txt
Μέγεθος:
1.74 KB
Μορφότυπο:
Item-specific license agreed upon to submission
Περιγραφή: