In conclusion, all the similarities between gpMucB and K-PI further support the idea that gpMucB contains a K-PI domain and considering that Echis carinatus venom is a complex mixture of toxins in which proteases strongly contribute to its toxicity, the K-PI activity can explain the direct anti-snake venom neutralization of MPE.
cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom.
1999, 2008) demonstrated that MPE is able to protect mice against the toxic and lethal effects provoked by the venom of Echis carinatus (family: Viperidae) through short and long term protection mechanisms.
Echis carinatus venom (EV) toxicity is mainly due to some proteases which affect blood coagulation.
Ecarin is a snake venom product from Echis carinatus
Blood chemistry of rats pretreated with Mucuna Pruriens seed aqueous extract MP101UJ after Echis Carinatus venom challenge.
Effects of Mucuna pruriens extract on activation of prothrombin by Echis carinatus venom.
Proteins from Mucuna pruriens and enzymes from Echis carinatus venom.
17) Isolated from the venom of the viper Echis carinatus
, ecarin cleaves prothrombin to generate meizothrom-bin.
The only anti-venom available in Abu Dhabi hospitals is Polyvalent Snake Antivenom (Equine), which contains immunoglobulin fraction in a sufficient quantity to neutralise 25 times the lethal dose of venom of six species of snakes, including Bitis Arietans, Cerastes Cerastes, Echis Carinatus
, Echis Coloratus, Naja Haje and Walterinnesia Aegyptia.