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Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: Queiroz,MR; Mamede,CC; Fonseca,KC; Canabrava,LCMN; França,LV; Silva,MC; Stanziola,L; Beletti,ME; Canabrava,HAN; Oliveira,F.
A myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a molecular weight of 16,500. BmooMtx induced release of creatine kinase and morphological analyses indicated that it provoked an intense myonecrosis, with visible leukocyte infiltrate and damaged muscle cells 24 hours after injection. Anti-BmooMTx antibodies partially neutralized the myotoxic activity of BmooMtx and crude B. moojeni venom, as judged by determination of plasma creatine kinase levels and histological evaluation of skeletal muscle in mice. Anti-BmooMTx antibodies were effective in reducing the...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Bothrops moojeni; Hyperalgesia; Myotoxin; Edema.
Ano: 2011
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007