Proteômica e potencial da atividade trombolítica da propriedade desfibrinogenante, in vivo, do veneno da Serpente Amazônica Crotalus durissus ruruima (Houge 1965).
| dc.contributor.advisor | López-Lozano, Jorge Luis | |
| dc.contributor.author | Araújo, Thiago Ferreira de | |
| dc.contributor.referee | López-Lozano, Jorge Luis | |
| dc.creator.Lattes | http://lattes.cnpq.br/9118006062331527 | pt_BR |
| dc.date.accessioned | 2020-03-12T15:18:15Z | |
| dc.date.accessioned | 2024-09-05T17:29:52Z | |
| dc.date.available | 2020-03-13 | |
| dc.date.available | 2020-03-12T15:18:15Z | |
| dc.date.issued | 2008-12-30 | |
| dc.description.abstract | An 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, serinoproteinase | pt_BR |
| dc.description.resumo | Através 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, serinoprotease | pt_BR |
| dc.identifier.uri | https://ri.uea.edu.br/handle/riuea/2131 | |
| dc.language | por | pt_BR |
| dc.publisher | Universidade do Estado do Amazonas | pt_BR |
| dc.publisher.country | Brasil | pt_BR |
| dc.publisher.initials | UEA | pt_BR |
| dc.publisher.program | Programa de Pós-Graduação em Biotecnologia e Recursos Naturais | pt_BR |
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Nat. Toxins 10:221– 238. ZHANG Y. L., HERVIO L., STRANDBERG L. MADISON E. L. 1999. Distinct contributions of residue 192 to the specificity of coagulation and fibrinolytic serine proteases. J. Biol.Chem. 274: 7153–7156. 71 ZHANG, H. L., HAN, R., CHEN, Z. X., CHEN, B. W., GU, Z. L., REID, P. F., RAYMOND, L. N. & OIN, Z. H. 2006. OpIate and acetylcholine-independent analgesic actions of crotoxin isolated from Crotalus durissus terrificus venom. Toxicon 48: 175182. | pt_BR |
| dc.rights | Acesso Aberto | pt_BR |
| dc.rights | Atribuição-NãoComercial-SemDerivados 3.0 Brasil | * |
| dc.subject | Crotalus durissus ruruima | pt_BR |
| dc.subject | Trombina – símile | pt_BR |
| dc.subject | Atividade desfibrinogenante | pt_BR |
| dc.subject | Atividade coagulante | pt_BR |
| dc.subject | Serinoprotease | pt_BR |
| dc.subject.cnpq | Biotecnologia | pt_BR |
| dc.title | Proteômica e potencial da atividade trombolítica da propriedade desfibrinogenante, in vivo, do veneno da Serpente Amazônica Crotalus durissus ruruima (Houge 1965). | pt_BR |
| dc.type | Dissertação | pt_BR |