Purification and renal effects of phospholipase A2 isolated from Bothrops insularis venom
dc.contributor.author | Machado Braga M.D. | |
dc.contributor.author | Costa Martins A.M. | |
dc.contributor.author | Alves C.D. | |
dc.contributor.author | de Menezes D.B. | |
dc.contributor.author | Martins R.D. | |
dc.contributor.author | Ferreira Barbosa P.S. | |
dc.contributor.author | de Sousa Oliveira I.M. | |
dc.contributor.author | Toyama M.H. | |
dc.contributor.author | Toyama D.O. | |
dc.contributor.author | dos Santos Diz Filho E.B. | |
dc.contributor.author | Ramos Fagundes F.H. | |
dc.contributor.author | Fonteles M.C. | |
dc.contributor.author | Azul Monteiro H.S. | |
dc.date.accessioned | 2024-03-13T01:37:47Z | |
dc.date.available | 2024-03-13T01:37:47Z | |
dc.date.issued | 2008 | |
dc.description.abstract | Bothrops insularis venom contains a variety of substances presumably responsible for several pharmacological effects. We investigated the biochemical and biological effects of phospholipase A2 protein isolated from B. insularis venom and the chromatographic profile showed 7 main fractions and the main phospholipase A2 (PLA2) enzymatic activity was detected in fractions IV and V. Fraction IV was submitted to a new chromatographic procedure on ion exchange chromatography, which allowed the elution of 5 main fractions designated as IV-1 to IV-5, from which IV-4 constituted the main fraction. The molecular homogeneity of this fraction was characterized by high-performance liquid chromatography (HPLC) and demonstrated by mass spectrometry (MS), which showed a molecular mass of 13984.20 Da; its N-terminal sequence presented a high amino acid identity (up to 95%) with the PLA2 of Bothrops jararaca and Bothrops asper. Phospholipase A2 isolated from B. insularis (Bi PLA2 ) venom (10 μg/mL) was also studied as to its effect on the renal function of isolated perfused kidneys of Wistar rats (n=6). Bi PLA2 increased perfusion pressure (PP), renal vascular resistance (RVR), urinary flow (UF) and glomerular filtration rate (GFR). Sodium (%TNa+) and chloride tubular reabsorption (%TCl-) decreased at 120 min, without alteration in potassium transport. In conclusion, PLA2 isolated from B. insularis venom promoted renal alterations in the isolated perfused rat kidney. © 2007 Elsevier Ltd. All rights reserved. | |
dc.description.firstpage | 181 | |
dc.description.issuenumber | 2 | |
dc.description.lastpage | 190 | |
dc.description.volume | 51 | |
dc.identifier.doi | 10.1016/j.toxicon.2007.08.017 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.uri | https://dspace.mackenzie.br/handle/10899/37533 | |
dc.relation.ispartof | Toxicon | |
dc.rights | Acesso Restrito | |
dc.subject.otherlanguage | Bothrops insularis | |
dc.subject.otherlanguage | Phospholipase A2 | |
dc.subject.otherlanguage | Renal biological activity | |
dc.title | Purification and renal effects of phospholipase A2 isolated from Bothrops insularis venom | |
dc.type | Artigo | |
local.scopus.citations | 13 | |
local.scopus.eid | 2-s2.0-38349011304 | |
local.scopus.updated | 2024-05-01 | |
local.scopus.url | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=38349011304&origin=inward |