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Bbil-TX, a PLA 2 , was purified from  Bothriopsis bilineata  snake venom after only one chromatographic step using RP-HPLC on   μ  -Bondapak C-18 column. A molecular mass of 14243.8 Da was confirmed by Q-Tof Ultima API ESI/MS (TOF MS mode) mass spectrometry. The partial protein sequence obtained was then submitted to BLASTp, with the search restricted to PLA 2  from snakes and shows high identity values when compared to other PLA 2 s. PLA 2  activity was presented in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 25–37°C. Maximum PLA 2  activity required Ca 2+  and in the presence of Cd 2+ , Zn 2+ , Mn 2+ , and Mg 2+  it was reduced in the presence or absence of Ca 2+ . Crotapotin from  Crotalus durissus cascavella  rattlesnake venom and antihemorrhagic factor DA2-II from  Didelphis albiventris  opossum sera under optimal conditions significantly inhibit the enzymatic activity. Bbil-TX induces myonecrosis in mice. The fraction does not show a significant cytotoxic activity in myotubes and myoblasts (C2C12). The inflammatory events induced in the serum of mice by Bbil-TX isolated from  Bothriopsis bilineata  snake venom were investigated. An increase in vascular permeability and in the levels of TNF-a, IL-6, and IL-1 was was induced. Since Bbil-TX exerts a stronger proinflammatory effect, the phospholipid hydrolysis may be relevant for these phenomena.

Biochemical, Pharmacological, and Structural Characterization of New Basic Bbil-TX fromBothriopsis bilineataSnake Venom