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Then, we assayed the residual activity of phospholipases A<jats:sub>2<\/jats:sub> (PLA<jats:sub>2<\/jats:sub>),metalloproteinases, and phosphodiesterases, abundant in <jats:italic>crotaline<\/jats:italic> snake venoms and relevant in the pathophysiology of envenomation, characterized by hemorrhage, pain, and tissue damage. <jats:italic>C. atrox<\/jats:italic> venom phospholipase A<jats:sub>2<\/jats:sub> and metalloproteinases were consistently and irreversibly inactivated by direct current (between 0 and 0.7 mA) exposure. In contrast, <jats:italic>C. atrox<\/jats:italic> venom phosphodiesterases were not affected. Total protein content and temperature of the sample remained the same. Secretory pancreatic phospholipase A<jats:sub>2<\/jats:sub>, homologue to snake venom phospholipases A<jats:sub>2<\/jats:sub>, was also inactivated by direct current treatment. In order to understand the structural reasoning behind PLA<jats:sub>2<\/jats:sub> inactivation, circular dichroism measurements were conducted on homogeneous commercial pancreatic phospholipase A<jats:sub>2<\/jats:sub>, and it was found that the enzyme undergoes structural alterations upon direct current exposure. \u00a9 2007 Wiley Periodicals, Inc. J Biochem Mol Toxicol 21:7\u201312, 2007; Published online in Wiley InterScience (<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.interscience.wiley.com\">www.interscience.wiley.com<\/jats:ext-link>). 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