Show simple item record

dc.creatorSoares, Andreimar Martins
dc.creatorAndrião Escarso, Silvia H.
dc.creatorBortoleto, Raquel K.
dc.creatorRodrigues Simioni, Lea
dc.creatorArni, Raghuvir K.
dc.creatorWard, Richard John
dc.creatorGutiérrez, José María
dc.creatorGiglio, José Roberto
dc.date.accessioned2017-01-31T15:08:54Z
dc.date.available2017-01-31T15:08:54Z
dc.date.issued2001-03-15
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0003986100922446es_ES
dc.identifier.issn0003-9861
dc.identifier.urihttp://hdl.handle.net/10669/29474
dc.description.abstractPiratoxins (PrTX) I and III are phospholipases A2 (PLA2s) or PLA2 homologue myotoxins isolated from Bothrops pirajai snake venom, which also induce myonecrosis, bactericidal activity against Escherichia coli, disruption of artificial membranes, and edema. PrTX-III is a catalytically active hemolytic and anticoagulant Asp49 PLA2, while PrTX-I is a Lys49 PLA2 homologue, which is catalytically inactive on artificial substrates, but promotes blockade of neuromuscular transmission. Chemical modifications of His, Lys, Tyr, and Trp residues of PrTX-I and PrTX-III were performed, together with cleavage of the N-terminal octapeptide by CNBr and inhibition by heparin and EDTA. The lethality, bactericidal activity, myotoxicity, neuromuscular effect, edema inducing effect, catalytic and anticoagulant activities, and the liposome-disruptive activity of the modified toxins were evaluated. A complex pattern of functional differences between the modified and native toxins was observed. However, in general, chemical modifications that significantly affected the diverse pharmacological effects of the toxins did not influence catalytic or membrane disrupting activities. Analysis of structural changes by circular dichroism spectroscopy demonstrated significant changes in the secondary structure only in the case of N-terminal octapeptide cleavage. These data indicate that PrTX-I and PrTX-III possess regions other than the catalytic site, which determine their toxic and pharmacological activities.es_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo//FAPESP/Brasiles_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceArchives of Biochemistry and Biophysics; Volumen 387, Número 2. 2001es_ES
dc.subjectBothrops Pirajaies_ES
dc.subjectMyotoxinses_ES
dc.subjectPhospholipases A2es_ES
dc.subjectPharmacological Activitieses_ES
dc.subjectChemical Modificationses_ES
dc.subjectCircular Dichroismes_ES
dc.subjectCrystal Structurees_ES
dc.subjectSnake venomes_ES
dc.titleDissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases A2 from Bothrops pirajai snake venomes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1006/abbi.2000.2244
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid11370840


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record