Comparative Biochemical Studies of Myotoxic Phospholipase A2 From Bothrops Venom

Authors: Toyama M.H.; Soares A.M.; Andriao-Escarso S.H.; Novello J.C.; Oliveira B.; Giglio J.R.; Fontes M.R.M.; Marangoni S.

Source: Protein and Peptide Letters, Volume 8, Number 3, June 2001 , pp. 179-186(8)

Publisher: Bentham Science Publishers

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Abstract:

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

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409445

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