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dc.contributor.authorAraújo, Thiago Ferreira de-
dc.date.available2020-03-13-
dc.date.available2020-03-12T15:18:15Z-
dc.date.issued2008-12-30-
dc.identifier.urihttp://repositorioinstitucional.uea.edu.br//handle/riuea/2269-
dc.description.abstractAn electrophoretic analysis, 1 – DE and 2 – DE, were detected of the venom of Crotalus durissus ruruima proteins with molecular masses of ~ 14, 32 and 50 kDA. By electrophoresis, SDS-PAGE tricine was detected a protein band of molecular mass of ~ 5 kDA that it suggests to understand to the crotamine. The activities phospholipase A2 and coagulant activity had been also detected in the venom of Crotalus durissus ruruima. Fractions of the venom of Crotalus durissus ruruima with coagulant activity, in vitro, under human fibrinogen and human plasma had been gotten by chromatography molecular exclusion and reverse phase. The coagulant activity gotten by the fractions was inhibited alone by PMSF, suggesting that the responsible toxin for the coagulant activity is one serinoproteinase. The proteolitic activity gotten by zimogram, using as bovine fibrinogen substratum, suggests the presence enzyme thrombin – like with molecular masses of the ~ 25 – 40 kDA. Of the coagulants, fractions gotten by chromatography reverse phase fraction (fraction 09) only presented defibrinating activity, in vivo, evaluated in mouse. This activity was not inhibited, in vivo, when this fraction previously was mix with human serum. Key words: Crotalus durissus ruruima, thrombin – like, defibrinating activity, coagulant activity, serinoproteinasept_BR
dc.languageporpt_BR
dc.publisherUniversidade do Estado do Amazonaspt_BR
dc.rightsAcesso Abertopt_BR
dc.rightsAtribuição-NãoComercial-SemDerivados 3.0 Brasil*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/br/*
dc.subjectCrotalus durissus ruruimapt_BR
dc.subjectTrombina – símilept_BR
dc.subjectAtividade desfibrinogenantept_BR
dc.subjectAtividade coagulantept_BR
dc.subjectSerinoproteasept_BR
dc.titleProteômica e potencial da atividade trombolítica da propriedade desfibrinogenante, in vivo, do veneno da Serpente Amazônica Crotalus durissus ruruima (Houge 1965).pt_BR
dc.typeDissertaçãopt_BR
dc.date.accessioned2020-03-12T15:18:15Z-
dc.contributor.advisor1López-Lozano, Jorge Luis-
dc.contributor.advisor1Latteshttp://lattes.cnpq.br/6251525203051399pt_BR
dc.contributor.referee1López-Lozano, Jorge Luis-
dc.contributor.referee1Latteshttp://lattes.cnpq.br/6251525203051399pt_BR
dc.creator.Latteshttp://lattes.cnpq.br/9118006062331527pt_BR
dc.description.resumoAtravés de análises por técnicas de eletroforese, uni e bidimensional, foram detectadas no veneno de Crotalus durissus ruruima proteínas com massas moleculares de ~ 14, 32 e 50 kDA. Por eletroforese SDS – PAGE TRIS – TRICINA foi detectada uma banda protéica de massa molecular de ~ 5 kDA que sugere compreender à crotamina. As atividades fosfolipase A2 e atividade coagulante também foram detectadas no veneno de Crotalus durissus ruruima. Frações do veneno de Crotalus durissus ruruima com atividade coagulante, in vitro, sob fibrinogênio e plasma humano foram obtidas por técnicas cromatográficas de filtração molecular e fase reversa. A atividade coagulante obtida pelas frações foi inibida só por PMSF, sugerindo que a toxina responsável pela atividade coagulante seja uma serinoprotease. A atividade proteolítica obtida por zimograma, utilizando como substrato fibrinogênio bovino, sugere a presença de enzimas trombina – símile com massas moleculares de ~ 25 a 40 kDA. Das frações coagulantes obtidas por cromatografia fase reversas somente uma fração (fração 09) apresentou atividade desfibrinogenante, in vivo, avaliada em camundongo. Essa atividade não foi inibida, in vivo, quando essa fração foi previamente incubada com soro humano. Os resultados sugerem que a atividade proteolítica do veneno de Crotalus durissus ruruima seja uma serinoprotease com potencial biotecnológico, como um possível antitrombolítico. Palavras Chaves: Crotalus durissus ruruima, trombina – símile, atividade desfibrinogenante, atividade coagulante, serinoproteasept_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.programPrograma de Pós-Graduação em Biotecnologia e Recursos Naturaispt_BR
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dc.subject.cnpqBiotecnologiapt_BR
dc.publisher.initialsUEApt_BR
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