Purification and partial characterization of two phospholipases A(2) from Bothrops leucurus (white-tailed-jararaca) snake venom
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2007-03-01
Autores
Higuchi, Debora Ayame
Barbosa, Christiano Marcello Vaz
Bincoletto, Claudia
Chagas, Jair Ribeiro
Magalhaes, Arinos
Richardson, Michael
Sanchez, Eladio Flores
Pesquero, João Bosco [UNIFESP]
Araújo, Ronaldo de Carvalho
Pesquero, Jorge Luiz
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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 Ca2+-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. (c) 2006 Elsevier Masson SAS. All rights reserved.
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Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 89, n. 3, p. 319-328, 2007.