Isolation And Characterization Of Papain-Like Cysteine Proteinases From Morinda Citrifolia Seed With Anti-Toxoplasmose Effect

dc.contributorSantiago, Fernanda Maria
dc.contributorhttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4769119A0
dc.contributorNaves, Karinne Spirandelli Carvalho
dc.contributorhttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4762339J3
dc.contributorJunior, Jair Pereira da Cunha
dc.contributorhttp://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4795802Y5
dc.creatorMota, Danielly Christine Adriani Maia
dc.date2018-01-24T18:14:06Z
dc.date2018-01-24T18:14:06Z
dc.date2017-12-20
dc.date.accessioned2023-09-28T20:44:52Z
dc.date.available2023-09-28T20:44:52Z
dc.identifierMOTA, 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.
dc.identifierhttps://repositorio.ufu.br/handle/123456789/20358
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/9057524
dc.descriptionCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.descriptionCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.descriptionTrabalho de Conclusão de Curso (Graduação)
dc.descriptionMorinda 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherUniversidade Federal de Uberlândia
dc.publisherBrasil
dc.publisherBiomedicina
dc.rightsAcesso Aberto
dc.subjectMorinda citrifolia
dc.subjectCysteine protease
dc.subjectproteolytic activity
dc.subjectToxoplasma gondii
dc.subjectCNPQ::CIENCIAS DA SAUDE
dc.titleIsolation And Characterization Of Papain-Like Cysteine Proteinases From Morinda Citrifolia Seed With Anti-Toxoplasmose Effect
dc.typeTrabalho de Conclusão de Curso


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