Thus, inhibition of proteolytic enzymes is important when thinking about molecules with antiophidic activity. Snake venoms are rich in several proteolytic enzymes that degrade a wide variety of natural substrates, such as casein, Benzyl alcohol fibrinogen and collagen, among others. It is known that several hemorrhagic and defibrinogenating toxins in snake venoms show significant activity against these substrates. Consequently, one of the first tests performed in this study was the inhibition of proteolytic activity of B. jararaca venom. The results obtained in this study revealed that the extract efficiently inhibited the venom proteolytic activity on azocasein, inhibiting completely the activity at higher concentrations. This result indicates a significant inhibitory action upon SVSPs and/or SVMPs. The blood incoagulability produced by Bothrops envenomation is associated with the combined action of diverse toxins, such as Irisflorentin Fibrinogenolytic enzymes, snake venom thrombin like enzymes and clotting factors activators, which are all proteases. The inhibition of these toxins could contribute for the inhibition of the blood incoagulability scenario. So, in view of the anti-proteolytic activity presented by the extract, the possible inhibitory role in blood incoagulability was investigated. Fibrinogenolytic enzymes are toxins that directly split off fragments mostly from the C terminal regions of Aa,B b and c chains of fibrinogen molecule, rendering it unclottable by thrombin. These enzymes do not convert fibrinogen to fibrin and the produced fibrinogen degradation products usually differ from those produced by plasmin. Fibrinogenolytic enzymes exert defibrinogenating action in vivo by consuming the circulant fibrinogen, contributing to the consumption coagulopathy. Since the fibrinogen levels are rapidly reduced, the patient tends to present blood incoagulability and prolonged clotting time. As could be observed in Figure 2, the aqueous leaf extract of J. gossypiifolia was able to inhibit fibrinogenolytic enzymes from B. jararaca. The extract, at higher concentrations, protected the fibrinogen from the proteolytic action from venom, protecting its Aa and Bb chains.