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dc.creatorSoares, Andreimar Martins
dc.creatorMancin, Adriana C.
dc.creatorCecchini, Alessandra L.
dc.creatorArantes, Eliane Candiani
dc.creatorFrança, Suzelei C.
dc.creatorGutiérrez, José María
dc.creatorGiglio, José Roberto
dc.date.accessioned2017-02-02T15:08:06Z
dc.date.available2017-02-02T15:08:06Z
dc.date.issued2001-09-01
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S1357272501000656es_ES
dc.identifier.issn1357-2725
dc.identifier.urihttp://hdl.handle.net/10669/29480
dc.description.abstractCrotoxin B, the basic Asp49-PLA2 subunit from crotoxin, the main component of Crotalus durissus terrificus venom, displays myotoxic, edema-inducing, bactericidal (upon Escherichia coli), liposomal-disrupting and anticoagulant activities. Chemical modifications of His (with 4-bromophenacyl bromide, BPB), Tyr (with 2-nitrobenzenesulphonyl fluoride, NBSF), Trp (with o-nitrophenylsulphenyl chloride, NPSC) and Lys (with acetic anhydride) residues of this protein, in addition to cleavage with cyanogen bromide (CNBr) and inhibition with ethylenediaminetetraacetic acid (EDTA), were carried out in order to study their effects on enzymatic and pharmacological activities. Lethality was reduced after modification of His or Lys residues, as well as after cleavage with CNBr, while enzymatic activity was completely abolished after modification of His or incubation with EDTA. Modification of Lys or Tyr, or cleavage with CNBr, partially reduced enzymatic activity. Anticoagulant activity was modified similarly to enzymatic activity, evidencing the dependency of this pharmacological effect on catalytic activity. Myotoxicity was reduced after modification of His or Lys, as well as after cleavage with CNBr, whereas EDTA reduced this effect to a lesser extent. Bactericidal effect was significantly reduced only after modification of Lys and after cleavage with CNBr. Edema-inducing activity was partially inhibited after treatment with EDTA and strongly reduced after acetylation of Lys residues and cleavage with CNBr, being only partially reduced after His alkylation. On the other hand, liposome disrupting activity was only partially reduced after modification of His and Tyr or after cleavage with CNBr. Modification of Trp residue partially reduced lethality and myotoxicity but did not affect enzymatic or anticoagulant activities. These data indicate that enzymatic activity is relevant for some pharmacological effects induced by crotoxin B (mainly lethal, myotoxic and anticoagulant activities), and also evidence that this subunit of crotoxin displays regions different from the active catalytic site which are involved in some of the toxic and pharmacological effects induced by this phospholipase A2.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.language.isoen_USes_ES
dc.sourceThe International Journal of Biochemistry & Cell Biology; Volumen 33, Número 9. 2001es_ES
dc.subjectCrotalus durissus terrificuses_ES
dc.subjectCrotoxin Bes_ES
dc.subjectMyotoxic phospholipase A2es_ES
dc.subjectBactericidal actiones_ES
dc.subjectPharmacological activitieses_ES
dc.subjectChemical modificationses_ES
dc.titleEffects of chemical modifications of crotoxin B, the phospholipase A2 subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activitieses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/S1357-2725(01)00065-6
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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