Por favor, use este identificador para citar o enlazar este ítem:
https://repositorio.ufu.br/handle/123456789/27634| ORCID: |  http://orcid.org/0000-0002-6357-4357 |
| Tipo de documento: | Trabalho de Conclusão de Curso |
| Tipo de acceso: | Acesso Aberto |
| Título: | Purificação e caracterização biológica de enzimas de 62 kDa do látex de Synadenium carinatum |
| Título (s) alternativo (s): | Purification and biological characterization of 62 kDa enzymes from Synadenium carinatum latex |
| Autor: | Ribeiro, Amanda Goulart |
| Primer orientador: | Ramos, Eliézer Lucas Pires |
| Primer coorientador: | Mota, Caroline Martins |
| Primer miembro de la banca: | Naves, Karinne Spirandelli Carvalho |
| Segundo miembro de la banca: | Cunha Júnior, Jair Pereira da |
| Resumen: | Background: 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. |
| Palabras clave: | Synadenium carinatum Proteases Fibrinogenolytic activity Toxoplasma gondii |
| Área (s) del CNPq: | CNPQ::CIENCIAS BIOLOGICAS::IMUNOLOGIA |
| Idioma: | eng |
| País: | Brasil |
| Editora: | Universidade Federal de Uberlândia |
| Cita: | RIBEIRO, 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. |
| URI: | https://repositorio.ufu.br/handle/123456789/27634 |
| Fecha de defensa: | 10-jul-2019 |
| Aparece en las colecciones: | TCC - Ciências Biológicas (Uberlândia) |
Ficheros en este ítem:
| Fichero | Descripción | Tamaño | Formato | |
|---|---|---|---|---|
| PurificationAndBiological.pdf | TCC | 483.28 kB | Adobe PDF |  Visualizar/Abrir |
Este ítem está sujeto a una licencia Creative Commons Licencia Creative Commons
