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dc.creatorAndrião Escarso, Silvia H.
dc.creatorSoares, Andreimar Martins
dc.creatorRodrigues, Veridiana M.
dc.creatorAngulo Ugalde, Yamileth
dc.creatorDíaz Oreiro, Cecilia
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorGiglio, José Roberto
dc.date.accessioned2017-01-30T20:53:00Z
dc.date.available2017-01-30T20:53:00Z
dc.date.issued2000-08
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0300908400011500es_ES
dc.identifier.issn0300-9084
dc.identifier.urihttp://hdl.handle.net/10669/29470
dc.description.abstractVenoms from eight Bothrops spp. were fractionated by ion-exchange chromatography on CM-Sepharose at pH 8.0 for the purification of myotoxins. Chromatographic profiles showed differences regarding myotoxic components among these venoms. B. alternatus, B. atrox and B. jararaca venoms did not show the major basic myotoxic fractions identified in the other venoms. Polyacrylamide gel electrophoresis for basic proteins also showed distinct patterns for these toxins. In vivo, all the isolated myotoxins induced release of creatine kinase due to necrosis of muscle fibers, accompanied by polymorphonuclear cell infiltration, and edema in the mouse paw. In addition, the toxins showed cytotoxic and liposome-disrupting activities in vitro. B. jararacussu bothropstoxins-I (BthTX-I) and II (BthTX-II) were submitted to chemical modifications of: His, by 4-bromophenacyl bromide (BPB) or photooxidation by Rose Bengal (RB); Tyr, by 2-nitrobenzenesulphonyl fluoride (NBSF); and Trp, by o-nitrophenylsulphenyl chloride (NPSC). The myotoxic and cytotoxic activities of BthTX-I, a Lys49 PLA2 homologue, after modification by BPB, RB, NBSF and NPSC, were reduced to 50%, 20%, 75%, 65% and 13%, 0.5%, 76%, 58%, respectively. However, the edema-inducing and liposome-disrupting activities were not significantly reduced by the above modifications. BPB-treated BthTX-II, an Asp49 PLA2 homologue, lost most of its catalytic, indirect hemolytic, anticoagulant, myotoxic and cytotoxic activities. The edema-inducing and liposome-disrupting activities were reduced to 50% and 80%, respectively. Lethality caused by BthTX-I and -II was strongly reduced after treatment with BPB or RB, but only partially with NBSF or NPSC. BthTX-I and -II, both native or modified, migrated similarly in a charge-shift electrophoresis. Antibodies raised against BthTX-I or -II, B. asper Basp-II and the C-terminal 115-129 peptide from Basp-II did not show significant differences in their cross-reactivity with the modified toxins, except with RB photooxidized toxins.es_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//FAPESP/Brasiles_ES
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Tecnológicas de Costa Rica/[FO-013-98]/CONICIT/Costa Ricaes_ES
dc.description.sponsorshipInternational Foundation for Science/[F/2766-1]/IFS/Sueciaes_ES
dc.language.isoen_USes_ES
dc.sourceBiochimie; Volumen 82, Número 8. 2000es_ES
dc.subjectBothrops venomses_ES
dc.subjectMyotoxinses_ES
dc.subjectPhospholipases A2es_ES
dc.subjectPharmacological Activityes_ES
dc.subjectChemical Modificationses_ES
dc.titleMyotoxic phospholipases A2 in Bothrops snake venoms: Effect of chemical modifications on the enzymatic and pharmacological properties of bothropstoxins from Bothrops jararacussues_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/S0300-9084(00)01150-0
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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