dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:00:20Z
dc.date.accessioned2022-10-05T14:45:24Z
dc.date.available2014-05-20T14:00:20Z
dc.date.available2022-10-05T14:45:24Z
dc.date.created2014-05-20T14:00:20Z
dc.date.issued1998-01-01
dc.identifierCytobios. Cambridge: Faculty Press, v. 93, n. 373, p. 83-92, 1998.
dc.identifier0011-4529
dc.identifierhttp://hdl.handle.net/11449/21341
dc.identifierWOS:000075559400002
dc.identifier6045437265946340
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3895132
dc.description.abstractBenzidine and diamino benzidine (DAB) oxidation, typically performed by peroxidases, was demonstrated by light and electron microscopy in peroxisomes, mitochondria and membranous structures which occurred in close contact with urate crystals in Malpighian tubules of nymphs and adults of Triatoma infestans. Peroxisomes were predominantly identified in cells of the distal region of the tubules, which is engaged in excretory mechanisms. DAB oxidation in mitochondria, even in the absence of hydrogen peroxide, may indicate the existence of a mitochondrial peroxidase and possibly a cytochrome c peroxidase. The localization of the extracellular membranous structures appeared restricted to the lumen of the proximal region of the tubules and they were assumed to be remnants of endoplasmic reticulum containing peroxidases.
dc.languageeng
dc.publisherFaculty Press
dc.relationCytobios
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectperoxidases
dc.subjectMalpighian tubules
dc.subjectTriatoma infestans
dc.subjectDAB oxidation
dc.subjectlaminated concretions
dc.subjectperoxisomes
dc.titlePeroxidase activity in Malpighian tubules of Triatoma infestans Klug
dc.typeArtigo


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