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BrTX-I, a PLA 2 , was purified from  Bothrops roedingeri  venom after only one chromatographic step using reverse-phase HPLC on   μ  -Bondapak C-18 column. A molecular mass of 14358.69 Da was determined by MALDI-TOF mass spectrometry. Amino acid analysis showed a high content of hydrophobic and basic amino acids as well as 14 half-cysteine residues. The total amino acid sequence was obtained using SwissProt database and showed high amino acid sequence identity with other PLA 2  from snake venom. The amino acid composition showed that BrTX-I has a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA 2 . BrTX-I presented PLA 2  activity and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0, 35–45°C, and required Ca 2+ .  In vitro , the whole venom and BrTX-I caused a neuromuscular blockade in biventer cervicis preparations in a similar way to other  Bothrops  species. BrTX-I induced myonecrosis and oedema-forming activity analyzed through injection of the purified BrTX-I in mice. Since BrTX-I exerts a strong proinflammatory effect, the enzymatic phospholipid hydrolysis might be relevant for these phenomena; incrementing levels of IL-1, IL-6, and TNF  α   were observed at 15 min, 30 min, one, two, and six hours postinjection, respectively.

biomed research international

Biochemical Characterization and Pharmacological Properties of New Basic PLA2BrTX-I Isolated fromBothrops roedingeri(Roedinger's Lancehead) Mertens, 1942, Snake Venom