Abstract
Two proteins with phospholipase A 2 (PLA 2) activity were purified to homogeneity from Bothrops leucurus (white-tailed-jararaca) snake venom through three chromatographic steps: Conventional gel filtration on Sephacryl S-200, ion-exchange on Q-Sepharose and reverse phase on Vydac C4 HPLC column. The molecular mass for both enzymes was estimated to be approximately 14 kDa by SDS-PAGE. The N-terminal sequences (48 residues) show that one enzyme presents lysine at position 48 and the other an aspartic acid in this position, and therefore they were designated blK-PLA 2 and blD-PLA 2 respectively. blK-PLA 2 presented negligible levels of PLA 2 activity as compared to that of blD-PLA 2. The PLA 2 activity of both enzymes is Ca 2+-dependent. blD-PLA 2 did not have any effect upon platelet aggregation induced by arachidonic acid, ADP or collagen, but strongly inhibits coagulation and is able to stimulate Ehrlich tumor growth but not angiogenesis.
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