Consulta: creatorFacets:"Acosta,OC"
Registros recuperados: 2
Data/hora: 17/06/2024 03:57:47

Cross-neutralization of the coagulant activity of Crotalus durissus terrificus venom from the northeast of Argentina by bivalent bothropic antivenom
Provedor de dados: 80
Autores: Rodríguez,JP; Gay,CC; Fusco,LS; Gauna,MC; Acosta,OC; Leiva,LC.
Cross-neutralization of Crotalus durissus terrificus venom coagulant activity was tested using bivalent horse antivenom against Bothrops alternatus and Bothrops diporus venoms. Our in vitro and in vivo experiments showed that bothropic antivenom neutralizes the thrombin-like activity of crotalic snake venom and this cross-reaction was demonstrated by immunoassays either with whole venom or a purified thrombin-like enzyme. These results suggest common antigenic properties and, consequently, similar molecular structure among venom thrombin-like enzymes. Besides, they provide information that could be further used in the development of new antivenom formulations.
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Thrombin-like enzyme; Snake venom; Antivenoms; Immunological cross-reaction.
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000100015

An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
Provedor de dados: 80
Autores: Gómez,GN; Nerli,BB; Acosta,OC; Picó,GA; Leiva,LCA.
Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Partition; Snake toxins; Isolation; Phospholipase A2; Proteases.
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008