A.S. Kamiguti

Comparative study of nine Bothrops snake venoms from adult female snakes and their offspring

Venoms of seven different Bothrops species and three subspecies (B. alternatus, B. cotiara, B. erythromelas, B. jararaca, B. jararacussu, B. moojeni, B. neuwiedi paranaensis. B.n. pauloensis and B.n. urutu) obtained from individual mothers and their young were investigated. Biometrics of snakes and protein content, toxicity (LD50), SDS-PAGE, proteolytic and clotting activities of venoms were estimated. Comparison of venoms from female snakes and their respective newborn offspring were variable in protein content, toxicity, fibrinolytic/amidolytic/thrombin-like activities and in venom yield in relation to snake length. B.n. paranaensis and B.n. pauloensis possessed the most toxic venoms. Caseinolytic activity of all venoms from female snakes and procoagulant activity of their offspring were consistently high. Venoms of B. erythromelas mother and offspring had no amidolytic activity and the highest levels of factor X and prothrombin activators without thrombin-like action. In contrast, the venom of newborn B. cotiara possessed the highest thrombin-like activity whereas a B. jararacussu adult female did not posses any procoagulant activity. An extremely high procoagulant activity of the venom of newborn Bothrops specimens was demonstrated.

Reliability of the simple 20 minute whole blood clotting test (WBCT20) as an indicator of low plasma fibrinogen concentration in patients envenomed by Bothrops snakes

Reliability of the simple 20 minute whole blood clotting test (WBCT20) as an indicator of low plasma fibrinogen concentration in patients envenomed by Bothrops snakes. Toxicon 32, 1045-1050, 1994.--A simple whole blood clotting test (WBCT20) was assessed for its efficacy in determination of severe defibrinogenation in patients envenomed by Bothrops snakes in Brazil. There was a close relationship between the results of the WBCT20 and plasma fibrinogen levels in 69 moderately envenomed patients. The advantage of the WBCT20 over estimation of plasma fibrinogen concentrations in patients is that it is a simpler, faster and more reliable test. It is also of use in assessing the effectiveness of antivenom therapy in relation to the restoration of blood coagulability.

Haemostatic changes caused by the venoms of south american snakes

Changes in the haemostatic mechanism caused by venoms of Bothrops, Crotalus and Lachesis snakes from Central and South America in human accidents are reviewed. Changes in the blood coagulation mechanism could be found depending on the action of the venom on clotting factors.

Blood coagulation mechanism in the snakes Waglerophis merremii and Bothrops jararaca

Abstract 1. 1. The blood coagulation mechanism was investigated in the snakes Bothrops jararaca and Waglerophis merremii, using homologous and heterologous systems to study the clotting function. 2. 2. Whereas the extrinsic pathway was efficient in both species, evidences for the intrinsic activation was found only in W. merremii plasma. 3. 3. The results obtained in several tests suggest that at least traces of Hageman factor are present in this plasma, providing the formation of a significant amount of contact product, besides the activation of prekallikrein formed in the same plasma.

Effect of heparin on the coagulant action of snake venoms

Abstract The influence of heparin on the coagulant activity of Bothrops jararaca, B. atrox, Crotalus durissus terrificus, C. adamanteus, Lachesis muta and Vipera russelli venom was investigated. The in vitro results demonstrated that heparin in concentrations ranging from 0·1 to 200 units failed to delay clotting which was induced by the addition of 200 μg of thrombin-like venoms (per ml) to plasma or to fibrinogen. All these heparin concentrations, however, prolonged the clotting time of factor X activator fractions from V. russelli , B. atrox and B. jararaca venom. Heparin previously given to dogs intravenously in doses ranging from 15,000 to 200,000 units failed to prevent the defibrination induced by the thrombin-like activity of venoms. Consequently, the therapeutic use of heparin in human snake envenomation lacks physiopathological support.

The inactivating effect of Bothrops jararaca and Waglerophis merremii snake plasma on the coagulant activity of various snake venoms

Plasmas of the poisonous snake Bothrops jararaca and of the non-poisonous snake Waglerophis merremii were not clotted by various snake venoms. These plasmas also inactivated venom clotting activity on human plasma. This effect was absent in snake serum and in heated snake plasma. The active fraction was isolated by gel chromatography from B. jararaca plasma and corresponded to the fibrinogen-containing fractions. It is suggested that the inactivation by snake plasma of the venom coagulant activity might be due to a fibrinogen-bound complex or to fibrinogen itself.

Prothrombin and factor X activating properties of Bothrops erythromelas venom

The enzymatic properties of Factor II (FII) and Factor X (FX) activators from Bothrops erythromelas venom were investigated. Both activators were inhibited by ethylenediaminetetraacetate (EDTA) and 1,10-phenanthroline, and are thought to be metalloproteinases with molecular weights of 90 kDa and 70-90 kDa, respectively. The activity of the FII activator in the crude venom was about 30 times greater than that in Oxyuranus scutellatus venom and the level of FX activator activity, which was CA2+ ion dependent, was similar to that in Daboia russelli venom. The venom also had two haemorrhagic factors (58 and 105 kDa) and two fibrinolytic enzymes (18 and 58 kDa).

The anticoagulant effect of Bothrops castelnaudi snake venom (Castelnaud's pit viper)

An inhibitory effect of Bothrops castelnaudi venom was observed on the following systems: prothrombin time, activated partial thromboplastin time, thrombin time, thromboplastin generation time, activation of factor X by Russells viper venom and Russells viper venom activated factor X (factor Xa). This effect did not require previous incubation and was prevented by the addition of Bothrops-antivenom. The prolonged activated partial thromboplastin time was not shortened by increased phospholipid concentration (0.5-10 mg/ml), suggesting that the inhibitory effect is not due to an anti-phospholipid activity. No significant fibrinogenolytic activity was detected upon incubation of human fibrinogen with the venom, since physiological levels of thrombin-clottable material were still present. Compared to Bothrops jararaca venom, the proteolytic activity on casein and on azocoll was very low. Thrombin-induced clots of human plasma and fibrinogen were not lysed by the venom within 24 hr. The results indicate that the anticoagulant effect of Bothrops castelnaudi venom is exerted at least at two levels of the blood coagulation mechanism: (1) before prothrombin activation, by inhibiting factor X-activation and factor Xa activity; (2) by direct action on thrombin.

An investigation of the coagulant activity of the venom of the saw-scaled viper (Echis carinatus) from Saudi Arabia

Unlike the venom of Echis carinatus from India, Pakistan, Nigeria, Kenya, Iran and Oman, Saudi Arabian E. carinatus venom is a poor activator of prothrombin. However, it possesses similar defibrinogenating activity to the other venoms. This is because the venom from Saudi Arabian snakes contains a calcium-dependent factor X activator. It is suggested that in future studies of the coagulant activity of venoms, the determination of plasma coagulant activity should be carried out in the presence of added calcium ions. This applies particularly to those venoms which do not act on plasma or fibrinogen, but which do cause in vivo defibrinogenation.