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Comparative Biochemical Studies of Myotoxic Phospholipase A2 From Bothrops Venom

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Venoms from Bothrops jararcussu Bothrops asper Bothrops atrox Bothrops pirajai Bothrops moojeni Bothrops alternatus and Bothrops (Bothriopasis) bilineata were fractionated using a simplified procedure based on-exchange chromatography on CM-Sepharose at pH 8.0 or reverse phase HPLC.The resulting elution profilesshowed important differences in the myotoxin contentof these venoms.The venoms froms B.alternatus,B.atrox and Bothriopsis bilineata did not contain the major myotoxin found in the other venoms.The amino acid sequences of the first 50 residues of the N-terminal region of the PLA2-Like mytoxins showed a homology of 90-96percent with other bothropic myotoxins.All of the myotoxins isolated induced rat paw edema, increased the level of plasma ceratine kinase and produced myonecrosis together with polymorphoniclear cell infiltration.

Keywords: Bothrops Bothriopsis; Bothrops Venom; Bothrops alternatus; Bothrops asper; Bothrops atrox; Bothrops jararcussu; Bothrops moojeni; Bothrops pirajai; Myotoxic Phospholipase A2; blineata

Document Type: Review Article


Publication date: 2001-06-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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