The herein invention refers to a purifying process of soluble proteins of the L. obliqua bristles through prothrombin activation; a partial deterrination of the amino acids sequence of the prothrombin activator; a process for determining the fraction II of the prothrombin activation as well as the N-terminal sequence and the sequence of internal fragments of the prothrombin activator fraction, the prothrombin activator and the utilization of the prothrombin activator through the homogenization of the L. obliqua bristles. The herein invention has shown that only one component of the Lonomia obliqua
venom, the Lopap, causes the hemorrhagic syndrome directly by activating prothrombin and, therefore, a patient should be conducted to a therapy when in contact with the Lonomia obliqua
venom. According to the herein invention, Lopap is a new prothrombin activator, showino to be a quite important factor responsible for consumption
coagulopathy, found in patients exposed to the
venom of the L. obliqua
caterpillar. In low doses of purified
protein, due to its capacity of activating prothrombin and generating
thrombin, it is possible, in controlled conditions, to withdraw
fibrinogen from circulation, transforming it in
fibrin microthrombs. The decrease on the concentration of plasmatic
fibrinogen promotes the increasing of
blood coagulation time and therefore it will avoid acute
vascular thrombosis. Since
protein does not present proteolytic activity, it could maintain the coagulating capacity of the
fibrinogen not consumed in the process. The fibrinogen plasmatic concentration would decrease, however there would not be predisposition for hemorrhagic state. Besides that, it could be used to produce diagnosis KITS for detecting dysprothrombinemias.