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Four basic PLA<jats:sub>2<\/jats:sub>s (pMTX-I to -IV) were purified from crude venom by a single-step chromatography using a CM-Sepharose ion-exchange column (1.5 \u00d7 15\u2009cm). Analysis of the N-terminal sequence demonstrated that pMTX-I and III belong to the catalytically active Asp49 phospholipase A<jats:sub>2<\/jats:sub>subclass, whereas pMTX-II and IV belong to the enzymatically inactive Lys49 PLA<jats:sub>2<\/jats:sub>s-like subclass. The PLA<jats:sub>2<\/jats:sub>s isolated from Panama<jats:italic>Bothrops asper<\/jats:italic>venom (pMTX-I, II, III, and IV) are able to induce myotoxic activity, inflammatory reaction mainly leukocyte migration to the muscle, and induce J774A.1 macrophages activation to start phagocytic activity and superoxide production.<\/jats:p>","DOI":"10.1155\/2013\/789689","type":"journal-article","created":{"date-parts":[[2012,12,24]],"date-time":"2012-12-24T21:01:00Z","timestamp":1356382860000},"page":"1-9","source":"Crossref","is-referenced-by-count":11,"title":["Biochemical Characterization, Action on Macrophages, and Superoxide Anion Production of Four Basic Phospholipases A<sub><b>2<\/b><\/sub>from Panamanian<i>Bothrops asper<\/i>Snake Venom"],"prefix":"10.1155","volume":"2013","author":[{"given":"Aristides Quintero","family":"Rueda","sequence":"first","affiliation":[{"name":"Departamento de An\u00e1lises Cl\u00ednicas, Toxicol\u00f3gicas e Bromatol\u00f3gicas, Faculdade de Ci\u00eancias 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