Proteins found in venoms, especially of the Viperidae snake family, exert, often with a narrow specificity, activating, inactivating, or other converting effects on different components of the hemostatic and fibrinolytic systems, respectively. Some purified snake venom proteins have become valuable tools in basic research and in diagnostic procedures in hemostaseology. "Procoagulant" as well as "anticoagulant" venom components have been identified in in vitro test systems. "Procoagulant" snake venom components may cause in vivo, upon massive application as in the case of snake-bite of small prey animals, intravascular coagulation leading to circulatory arrest and rapid death. Smaller doses of procoagulant venom components applied to large organisms as in the case of snake-bite accidents in humans, may cause a consumption coagulopathy with localized or generalized bleeding. Highly purified, specific fibrinogen coagulant venom proteinases are used in human medicine to produce therapeutic defibrinogenation. These practically nontoxic venom enzymes may act synergistically with other components aggravating their toxic effects.