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dc.contributor.author
Fernandez Villamil, Silvia Hebe  
dc.contributor.author
Podestá, Dolores  
dc.contributor.author
Molina Portela, María Del Pilar  
dc.contributor.author
Stoppani, Andres  
dc.date.available
2019-07-11T16:16:38Z  
dc.date.issued
2001-12  
dc.identifier.citation
Fernandez 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; 249-256  
dc.identifier.issn
0166-6851  
dc.identifier.uri
http://hdl.handle.net/11336/79351  
dc.description.abstract
Crithidia 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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Crithidia Fasciculata  
dc.subject
Oxidative Damage  
dc.subject
Poly(Adp-Ribose)Polymerase  
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Trypanosomatids  
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Β--Lapachone  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-07-05T17:31:37Z  
dc.journal.volume
115  
dc.journal.number
2  
dc.journal.pagination
249-256  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina  
dc.description.fil
Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina  
dc.description.fil
Fil: Molina Portela, María Del Pilar. Universidad de Buenos Aires. Facultad de Medicina; Argentina  
dc.description.fil
Fil: Stoppani, Andres. Universidad de Buenos Aires. Facultad de Medicina; Argentina  
dc.journal.title
Molecular and Biochemical Parasitology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685101002912  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/S0166-6851(01)00291-2