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  • Title: Differences in distribution of myotoxic proteins in venoms from different Bothrops species.
    Author: Moura-da-Silva AM, Cardoso DF, Tanizaki MM.
    Journal: Toxicon; 1990; 28(11):1293-301. PubMed ID: 2128421.
    Abstract:
    Antigens with high myotoxic activity were isolated from Bothrops jararacussu venom by Sephadex G-75 and SP-Sephadex C-25. These antigens were recognized using western blotting by B. jararacussu, B. moojeni, B. neuwiedi and B. pradoi antivenoms, and weakly by B. jararaca antivenom. B. alternatus, B. atrox, B. cotiara and B. erythromelas antivenoms failed to recognize these antigens. Antisera raised against these antigens recognized bands with mol. wt around 18,000 in the venoms of B. jararacussu, B. moojeni, B. neuwiedi and B. pradoi and reacted in ELISA with non-denaturated B. jararaca venom. However it failed to react in ELISA with nondenatured B. alternatus, B. atrox, B. cotiara and B. erythromelas venoms. The myotoxicity induced by these crude venoms confirmed that these antigens are possibly the only major myotoxin as the levels of creatine phosphokinase activity in mice serum released by intramuscular injection of B. jararacussu, B. moojeni, B. neuwiedi and B. pradoi venoms (myotoxin +) were five to eight-fold higher than those obtained with B. alternatus, B. atrox, B. cotiara, B. erythromelas and B. jararaca venoms. Using the double immunodiffusion technique the myotoxins of B. jararacussu, B. neuwiedi and B. pradoi showed total identity while B. moojeni myotoxin behaved as a partially identical antigen.
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