Artículo
Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
Fernandez Villamil, Silvia Hebe
; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres
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Fecha de publicación:
12/2001
Editorial:
Elsevier Science
Revista:
Molecular and Biochemical Parasitology
ISSN:
0166-6851
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Articulos(INGEBI)
Articulos de INST.DE INVEST.EN ING.GENETICA Y BIOL.MOLECULAR "DR. HECTOR N TORRES"
Articulos de INST.DE INVEST.EN ING.GENETICA Y BIOL.MOLECULAR "DR. HECTOR N TORRES"
Citación
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
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