1. Repositório Institucional - Universidade Federal de Uberlândia
  2. Instituto de Ciências Biomédicas (ICBIM)
  3. TCC - Ciências Biomédicas
Please use this identifier to cite or link to this item: https://repositorio.ufu.br/handle/123456789/20358
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dc.creatorMota, Danielly Christine Adriani Maia-
dc.date.accessioned2018-01-24T18:14:06Z-
dc.date.available2018-01-24T18:14:06Z-
dc.date.issued2017-12-20-
dc.identifier.citationMOTA, Danielly Christine Adriani Maia. Isolation and characterization of papain-like cysteine proteinases from Morinda citrifolia seed with anti-toxoplasmose effect. 2017. 23 f. Trabalho de Conclusão de Curso (Graduação em Biomedicina) - Faculdade de Ciências Biomédicas, Universidade Federal de Uberlândia. Uberlândia, 2017.pt_BR
dc.identifier.urihttps://repositorio.ufu.br/handle/123456789/20358-
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
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.subjectMorinda citrifoliapt_BR
dc.subjectCysteine proteasept_BR
dc.subjectproteolytic activitypt_BR
dc.subjectToxoplasma gondiipt_BR
dc.titleIsolation And Characterization Of Papain-Like Cysteine Proteinases From Morinda Citrifolia Seed With Anti-Toxoplasmose Effectpt_BR
dc.typeTrabalho de Conclusão de Cursopt_BR
dc.contributor.advisor1Santiago, Fernanda Maria-
dc.contributor.advisor1Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4769119A0pt_BR
dc.contributor.referee1Naves, Karinne Spirandelli Carvalho-
dc.contributor.referee1Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4762339J3pt_BR
dc.contributor.referee2Junior, Jair Pereira da Cunha-
dc.contributor.referee2Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4795802Y5pt_BR
dc.creator.Latteshttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K8030220Y2pt_BR
dc.description.degreenameTrabalho de Conclusão de Curso (Graduação)pt_BR
dc.description.resumoMorinda citrifolia, known as Noni, is used in folk medicine with several therapeutic applications. The present study investigated the enzymatic and biological characteristics of the papain-like cysteine proteases (PLCP) from M. citrifolia seed. Its enzyme was purified in two-step by DEAE-Sephacel and Phenyl-Sepharose CL-4B (10 × 0.6 cm) columns. PLCP enzyme demonstrated an apparent molecular mass of 51 kDa on SDS-PAGE 14%. The proteolytic activity in the presence of fibrinogen with the PLPC of M. citrifolia demonstrated total hydrolysis of the fibrinogen chains, occurring in the concentration of 20 μg; with the optimum pH of 7.0; temperatures range from room temperature to 50°C; better activity with calcium ions and the effect of inhibition appeared in the presence of Leupeptin. There was no platelet aggregation or coagulation activity. PLCP enzyme was not cytotoxic for cells such as Human Foreskin Fibroblasts (HFF) and murine embryo fibroblasts strain NIH/Swiss (NIH/3T3) macrophages and showed to be effective when tested directly against Toxoplasma gondii infection in vitro. In that sense, this study indicates perspectives for pharmacological applications of M. citrifolia enzymes.pt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.courseBiomedicinapt_BR
dc.sizeorduration23pt_BR
dc.subject.cnpqCNPQ::CIENCIAS DA SAUDEpt_BR
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