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SILVA, F. de A.; LIOTTI, R. G.; BOLETI, A. P. de A.; REIS, E. de M.; PASSOS, M. B. S.; SANTOS, E. L. dos; SAMPAIO, O. M.; JANUÁRIO, A. H.; BRANCO, C. L. B.; SILVA, G. F. da; MENDONÇA, E. A. F. de; SOARES, M. A.. |
Tipo: Artigo de periódico |
Palavras-chave: Paullinia Cupana. |
Ano: 2018 |
URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1109579 |
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FRIHLING, B. E. F.; BOLETI, A. P. de A.; OLIVEIRA, C. F. R. de; SANCHES, S. C.; CARDOSO, P. H. de O.; VERBISCK, N. V.; MACEDO, M. L. R.; SANTA RITA, P. H.; CARVALHO, C. M. E.; MIGLIOLO, L.. |
Nature presents a wide range of biomolecules with pharmacological potential, including venomous animal proteins. Among the protein components from snake venoms, phospholipases (PLA2) are of great importance for the development of new anticancer compounds. Thus, we aimed to evaluate the PLA2 anticancer properties from Bothrops moojeni venom. The crude venom was purified through three chromatographic steps, monitored by enzymatic activity and SDS-PAGE (12%). The purified PLA2 denominated BmPLA2 had its molecular mass and N-terminal sequence identified by mass spectrometry and Edman degradation, respectively. BmPLA2 was assayed against human epithelial colorectal adenocarcinoma cells (Caco-2), human rhabdomyosarcoma cells (RD) and mucoepidermoid carcinoma of... |
Tipo: Artigo de periódico |
Palavras-chave: Biotecnologia; Espectrometria; Proteína; Animal proteins; Biotechnology; Bothrops; Cell membranes; Mass spectrometry; Phospholipase A2. |
Ano: 2022 |
URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743 |
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