BbMP-1, a new metalloproteinase isolated from Bothrops brazili snake venom with in vitro antiplasmodial properties
作者： Anderson M. Kayano , Rodrigo Simões-Silva , Patrícia S.M. Medeiros , Vinícius G. Maltarollo , Kathia M. Honorio
DOI: 10.1016/J.TOXICON.2015.09.005
关键词:
摘要: This study describes the biochemical and functional characterization of a new metalloproteinase named BbMP-1, isolated from Bothrops brazili venom. BbMP-1 was homogeneous on SDS-PAGE, presented molecular mass 22,933Da pI 6.4. The primary structure partially elucidated with high identity others metalloproteinases Viperidae venoms. enzymatic activity azocasein evaluated in different experimental conditions (pH, temperature). A significant reduction enzyme after exposure to chelators divalent cations (EDTA), reducing agents (DTT), pH less than 5.0 or temperatures higher 45 °C observed. showed fibrinogen degrading Aα chain quickly lesser extent Bβ chain. Also demostrated be weakly hemorrhagic, presenting however, myotoxic edematogenic activity. vitro against Plasmodium falciparum an IC50 3.2 ± 2.0 μg/mL. may help understand pathophysiological effects induced by this group toxin their participation symptoms observed cases snake envenomation. Moreover, result is representative for proteins shows biotechnological potential demonstration its antiplasmodial
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