Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
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 stabilit...
| Autores: | , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2001 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/79351 |
| Acesso em linha: | http://hdl.handle.net/11336/79351 |
| Access Level: | acceso abierto |
| Palavra-chave: | Crithidia Fasciculata Oxidative Damage Poly(Adp-Ribose)Polymerase Trypanosomatids Β--Lapachone https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Resumo: | 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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