Comparative biochemical studies of myotoxic phospholipase A(2) from Bothrops venom
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Data
2001-06-01
Autores
Toyama, M. H.
Soares, A. M.
Andriao-Escarso, S. H.
Novello, J. C.
Oliveira, B.
Giglio, JR
Fontes, MRM
Marangoni, S.
Título da Revista
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Título de Volume
Editor
Bentham Science Publ Ltd
Resumo
Venoms from Bothrops jararacussu, Bothrops asper, Bothrops atrox, Bothrops pirajai, Bothrops moojeni, Bothrops alternatus and Bothrops (Bothriopsis) bilineata were fractionated using a simplified procedure based on ion-exchange chromatography on CM-Sepharose at pH 8.0 or reverse phase HPLC. The resulting elution profiles showed important differences in the myotoxin content of these venoms. The venoms from B. alternatus, B. atrox and Bothriopsis bilineata did not contain the major myotoxin found in the other venoms. The amino acid sequence of the first 50 residues of the N-terminal region of the PLA(2)-like myotoxins showed a homology of 90-96% with other bothropic myotoxins. All of the myotoxins isolated induced rat paw edema, increased the level of plasma creatine kinase and produced myonecrosis together with polymorphonuclear cell infiltration.
Descrição
Palavras-chave
HPLC, Bothrops, phospholipase A(2), and myotoxin
Como citar
Protein and Peptide Letters. Hilversum: Bentham Science Publ Ltd, v. 8, n. 3, p. 179-186, 2001.