1. Repositório Institucional - Universidade Federal de Uberlândia
2. Instituto de Biologia (INBIO)
3. TCC - Ciências Biológicas (Uberlândia)

ORCID:	http://orcid.org/0000-0002-6357-4357
Document type:	Trabalho de Conclusão de Curso
Access type:	Acesso Aberto
Title:	Purificação e caracterização biológica de enzimas de 62 kDa do látex de Synadenium carinatum
Alternate title (s):	Purification and biological characterization of 62 kDa enzymes from Synadenium carinatum latex
Author:	Ribeiro, Amanda Goulart
First Advisor:	Ramos, Eliézer Lucas Pires
First coorientator:	Mota, Caroline Martins
First member of the Committee:	Naves, Karinne Spirandelli Carvalho
Second member of the Committee:	Cunha Júnior, Jair Pereira da
Summary:	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.
Keywords:	Synadenium carinatum Proteases Fibrinogenolytic activity Toxoplasma gondii
Area (s) of CNPq:	CNPQ::CIENCIAS BIOLOGICAS::IMUNOLOGIA
Language:	eng
Country:	Brasil
Publisher:	Universidade Federal de Uberlândia
Quote:	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
Date of defense:	10-Jul-2019
Appears in Collections:	TCC - Ciências Biológicas (Uberlândia)

This item is licensed under a Creative Commons License