Purification and renal effects of phospholipase A2 isolated from Bothrops insularis venom

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Machado Braga M.D.
Costa Martins A.M.
Alves C.D.
de Menezes D.B.
Martins R.D.
Ferreira Barbosa P.S.
de Sousa Oliveira I.M.
Toyama M.H.
Toyama D.O.
dos Santos Diz Filho E.B.
Ramos Fagundes F.H.
Fonteles M.C.
Azul Monteiro H.S.
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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.
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