Please use this identifier to cite or link to this item: https://repositorio.ufu.br/handle/123456789/27634
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dc.creatorRibeiro, Amanda Goulart-
dc.date.accessioned2019-12-12T22:27:49Z-
dc.date.available2019-12-12T22:27:49Z-
dc.date.issued2019-07-10-
dc.identifier.citationRIBEIRO, Amanda Goulart. Purification and biological characterization of 62 kDa enzymes from Synadenium carinatum latex. 2019. 20 f. Trabalho de Conclusão de Curso (Graduação em Ciências Biológicas) – Universidade Federal de Uberlândia, Uberlândia, 2019.pt_BR
dc.identifier.urihttps://repositorio.ufu.br/handle/123456789/27634-
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Uberlândiapt_BR
dc.rightsAcesso Abertopt_BR
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/*
dc.subjectSynadenium carinatumpt_BR
dc.subjectProteasespt_BR
dc.subjectFibrinogenolytic activitypt_BR
dc.subjectToxoplasma gondiipt_BR
dc.titlePurificação e caracterização biológica de enzimas de 62 kDa do látex de Synadenium carinatumpt_BR
dc.title.alternativePurification and biological characterization of 62 kDa enzymes from Synadenium carinatum latexpt_BR
dc.typeTrabalho de Conclusão de Cursopt_BR
dc.contributor.advisor-co1Mota, Caroline Martins-
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dc.contributor.advisor1Ramos, Eliézer Lucas Pires-
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dc.contributor.referee1Naves, Karinne Spirandelli Carvalho-
dc.contributor.referee1Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4762339J3&tokenCaptchar=03AOLTBLR8xJjTDyFgngQ12HktqtWgiZLUWWjCdKg75lznT4C4FLIvSZgAgfoEK7BukGq4kQ44IxWbECrTesgw_ZH8pPNdPDrIbcMcIJfNT0FAnbG9jOBWHP4XDGJBCFqocMb0UWHIAFk9Wi3RU_unXPUi-9Uh8-TUK9Ny0eq_VZCjWWItvO0SJzEqq8v5fKsDm8e9_r7N6ftLsC3pbhh25syPJgDdvnR5CR7JyzwuOpZUATdlp8cjvliXCM8ddTVlie33jK9DxOQaKATnpsmrAqhdzrlQr0XSpAwc99a3XZPsGnfZkgPApQBo3k2wbtBLwhbG6h-t1RbIwf3PgSxYab3RV8YsSHtODHl8qrjAU9-gFF1hOfyYcdU-pXNXF8Mmyy2tz-ewrgu8Lj5TwnXluJuJTN_ZBLJuFj2DS6qDm0TU6wtx8fgLq0-ukfsvjTMm17D4kKtxhpIVdVpt301q2fMTyLH1w1EqdQ_bieDeS3cGXbRXxT8b6R9DFsj4zy2vfZH7VyAVp4zJpt_BR
dc.contributor.referee2Cunha Júnior, Jair Pereira da-
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dc.creator.Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K8611454Y3&tokenCaptchar=03AOLTBLTQHFEFiLe-NhN2lJoJkcqduwDbpNzRtvCxRDTXLCmHHxGABqxkEpH6Ww42gKfEVlXQQOp5fr2s6QapOxg-U7HBl3W34luYPkVDfOahky8jqxaGy5LhgfZxyIIwhQTvEBosdHmNRDYAGgTh5He5ENUTWa7UY_4Duc0zJq-lJRuwNLFyUjKdjqhZUulSn_Zv5Z6Wc1DYLDK2LQsWe-8hdh9tcZwhXmEzR-bEY2YH-q_JlzlXrg5zrrM9RYIx8ox1xCwVHBuhcZOqTXcTK5jZbd_kvW47KZyeXVYYReqdadFUjB4xgX1Z1IcRiW_i-PHJYy3SRmm4QMUBYgU6Em1jsLoHhlNuqFCLj-NHuJz_KVjB6IWqj-JgRa76eCdcGngAH3KXZG3MnfTPpu3XSNyUYxTPdKtb6i5zolhlJVV4uetsw3s9YYgiBkEHdNUjaDrVvCyBt4jm3C2ymhHqEBBmx92N-Y3Ad_nTZ4cd-vDY2uOI56oC7ufbnkyJjvbkB8zGzf4jxl-Ypt_BR
dc.description.degreenameTrabalho de Conclusão de Curso (Graduação)pt_BR
dc.description.resumoBackground: Plant Proteases have been described in the literature as being able to interfere in biological processes and behaving as antitumor, antiinflammatory, anthelmintic and antifungal agents. The aim of the present work was the purification and characterization of Synadenium carinatum 62 kDa enzyme and evaluation of in antimicrobial and antiparasitic effects. Results: A 62 kDa serine protease with fibrinolytic activity was purified from S. carinatum latex by the combination of ion exchange and affinity chromatography. The 62 kDa enzyme showed high proteolytic activity on bovine fibrinogen at optimal pH 7,0 and 37 °C. The 62 kDa enzyme of S. carinatum degraded the fibrinogen α-chain and the β-chain, while the fibrinogen γ-chain remained unchanged. In the presence of protease inhibitors as benzamidine; leupeptin; PMSF; EDTA and phenanthroline the fibrinogenolytic activity of the S. carinatum 62 kDa enzyme was inhibited in the presence of the PMSF, suggesting that it is a member of the serine-proteases family. Interestingly, in the presence of EDTA, the enzyme had increased enzymatic activity. The fibrinogenolytic activity of the enzyme was inhibited in the presence of Cu²+ and Zn²+. In biological assays, the S. carinatum 62 kDa enzyme showed non-cytotoxic on peritoneal macrophages, murine bone-marrow-derived macrophages and fibroblasts. In addition, the enzyme showed antiparasitic activity on Toxoplasma gondii infection in vitro in high concentration. Conclusions: In that sense, this study sheds perspectives for future pharmacological applications of S. carinatum enzymes.pt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.courseCiências Biológicaspt_BR
dc.sizeorduration20pt_BR
dc.subject.cnpqCNPQ::CIENCIAS BIOLOGICAS::IMUNOLOGIApt_BR
dc.orcid.putcode65991587-
Appears in Collections:TCC - Ciências Biológicas (Uberlândia)

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