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Assessing the stability of historical and desiccated snake venoms from a medically important Ecuadorian collection

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dc.contributor.author de Almeida, José R.
dc.contributor.author Mendes, Bruno
dc.contributor.author Palma Patiño, Ricardo Sebastián
dc.contributor.author Pico, José
dc.contributor.author Laines, Johana
dc.contributor.author Terán, María
dc.contributor.author Salazar Mogollón, Noroska Gabriela
dc.contributor.author Zaruma Torres, Fausto
dc.contributor.author da Silva Caldeira, Cleópatra
dc.contributor.author da Silva, Saulo L.
dc.date.accessioned 2020-01-21T14:41:39Z
dc.date.available 2020-01-21T14:41:39Z
dc.date.issued 2020
dc.identifier.citation Almeida, J. R., Mendes, B., Patiño, R. S. P., Pico, J., Laines, J., Terán, M., … da Silva, S. L. (2020). Assessing the stability of historical and desiccated snake venoms from a medically important Ecuadorian collection. Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology, 230(January). doi.org/10.1016/j.cbpc.2020.108702 es
dc.identifier.uri http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/332
dc.identifier.uri https://doi.org/10.1016/j.cbpc.2020.108702
dc.description.abstract Bothrops asper and Bothrops atrox are important venomous snakes from Ecuador responsible for the most of ophidic accidents, which in the past were treated with a national polyvant antivenom. For years, the venom pools were collected and stored at room temperature in a laboratory. Taking into account the controversial ability of desiccated samples to retain their biological effects and enzymatic activities, we investigated the biochemical and toxicological properties of venoms after years of storage. The proteomic profiles of historical venoms analyzed by high-performance liquid chromatography and electrophoresis are very similar. The fresh batches of venom were more lethal than those stored for years, just as the initial and current LD50 values of these samples changed. Significant differences were showed in the myotoxic and hemorrhagic activity of some venom pools, while no significant statistical differences were found for the edema activity. The enzymatic assays revealed a variation in proteolytic activity on azocasein and phospholipase A2 activity, and low differences were reported for thrombin-like serine protease activity. The maintenance of the proteomic profile and certain toxicological activities convert this venom library in a valuable source for research purposes. Nonetheless, the significative reduction of toxicological activities, such as hemorrhagic activity not feasible using these samples for the antivenom production. es
dc.language.iso en es
dc.rights openAccess es
dc.subject Snake venom es
dc.subject Stability es
dc.subject Desiccated venom es
dc.subject Proteomic es
dc.subject Toxicological es
dc.title Assessing the stability of historical and desiccated snake venoms from a medically important Ecuadorian collection es
dc.type Article es


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