Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone

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dc.conicet.fuenteindividual
dc.conicet.organizacionConsejo Nacional de Investigaciones Científicas y Técnicas
dc.conicet.organizacionUniversidad de Buenos Aires. Facultad de Medicina
dc.conicet.organizacionUniversidad de Buenos Aires. Facultad de Medicina
dc.conicet.organizacionUniversidad de Buenos Aires. Facultad de Medicina
dc.conicet.organizacionUniversidad de Buenos Aires. Facultad de Medicina
dc.conicet.paisOrganizacionArgentina
dc.conicet.paisOrganizacionArgentina
dc.conicet.paisOrganizacionArgentina
dc.conicet.paisOrganizacionArgentina
dc.conicet.paisOrganizacionArgentina
dc.conicet.produccionid6340400
dc.contributor.authorFernandez Villamil, Silvia Hebe
dc.contributor.authorPodestá, Dolores
dc.contributor.authorMolina Portela, María Del Pilar
dc.contributor.authorStoppani, Andres
dc.date.accessioned2019-07-11T16:16:38Z
dc.date.available2019-07-11T16:16:38Z
dc.date.issued2001-12
dc.date.updated2019-07-05T17:31:37Z
dc.description.abstractCrithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD+ as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H2O2 Fenton system. β-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.es
dc.description.filFil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
dc.description.filFil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina
dc.description.filFil: Molina Portela, María Del Pilar. Universidad de Buenos Aires. Facultad de Medicina; Argentina
dc.description.filFil: Stoppani, Andres. Universidad de Buenos Aires. Facultad de Medicina; Argentina
dc.formatapplication/pdfes
dc.identifier.citationFernandez Villamil, Silvia Hebe; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres; Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone; Elsevier Science; Molecular and Biochemical Parasitology; 115; 2; 12-2001; 249-256es
dc.identifier.institucionalCONICET
dc.identifier.issn0166-6851es
dc.identifier.repoCONICET Digital
dc.identifier.urihttp://hdl.handle.net/11336/79351
dc.journal.ciudadAmsterdames
dc.journal.number2es
dc.journal.pagination249-256es
dc.journal.paisPaíses Bajoses
dc.journal.titleMolecular and Biochemical Parasitologyes
dc.journal.volume115es
dc.language.isoenges
dc.publisherElsevier Sciencees
dc.relation.alternativeidinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685101002912
dc.relation.alternativeidinfo:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/S0166-6851(01)00291-2
dc.rightsinfo:eu-repo/semantics/openAccess*
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/*
dc.subjectCrithidia Fasciculataes
dc.subjectOxidative Damagees
dc.subjectPoly(Adp-Ribose)Polymerasees
dc.subjectTrypanosomatidses
dc.subjectΒ--Lapachonees
dc.subject.classificationBioquímica y Biología Moleculares
dc.subject.classificationCiencias Biológicases
dc.subject.classificationCIENCIAS NATURALES Y EXACTASes
dc.titleCharacterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachonees
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion

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