The origin of snakes and evolution of the venom apparatus.

Action of snake venom components on the haemostatic system

The polyphyletic family Colubridae contains approximately two-thirds of the described species of advanced snakes, and nearly half of these (∼700 species) produce a venom in a specialized cephalic gland, the Duvernoy's gland. Biochemical and pharmacological information is lacking for venoms of most species, and modest detailed information on venom composition is available for only a few species which represent a potential health threat to humans. However, colubrid venoms represent a vast source of novel compounds, and some toxins, such as the 20–26 kD CRISP-related venom proteins (helveprins), have only recently been identified in both colubrid and elapid/viperid venoms. Difficulties associated with extraction have been addressed, and it is now possible to obtain venom sufficient for many analyses from even small species. There appears to be a greater number of venom components shared among the colubrids and the front-fanged snakes than has been previously noted, and it is probable that as analytical metho...

Biochemistry and pharmacology of colubrid snake venoms

Characterization of venom (Duvernoy's secretion) from twelve species of colubrid snakes and partial sequence of four venom proteins.

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.

Dietrich Mebs

Papers

Pharmacological and biochemical properties of a venom gland extract from the snake Thelotornis kirtlandi.