A novel C-lectin protein, lebecetin, was purified and characterized from the venom of Macrovipera lebetina. It is a disulfide-linked heterodimer of 15 and 16 kD. The subunits are homologous to each other and to the other snake venom proteins of the C-type (Ca(2+)-dependent) lectin superfamily. Lebecetin shows a potent inhibitory effect on whole blood and washed platelets induced by different ag...

Phospholipases type A2 (PLA2s) are the most abundant proteins found in Viperidae snake venom. They are quite fascinating from both a biological and structural point of view. Despite similarity in their structures and common catalytic properties, they exhibit a wide spectrum of pharmacological activities. Besides being hydrolases, secreted phospholipases A2 (sPLA2) are an important group of toxi...

The venoms extracted from a colubrid snake [Malpolon monspessulanus (Hermann)], seven viperids [Montivipera xanthina (Gray), Montivipera wagneri Nilson &Andrén, Vipera ammodytes (Linnaeus), Vipera kaznakovi (Nikolsky), Vipera eriwanensis (Bonaparte), Vipera barani Böhme & Joger, Macrovipera lebetina (Linnaeus)] and an elapid snake [Walterinnesia aegyptia (Lataste)] collected from various region...

Background:Envenomation by Macrovipera lebetina (M. lebetina) is characterized by prominent local tissue damage, hemorrhage, abnormalities in the blood coagulation system, necrosis, and edema. However, the main cause of death after a bite by M. lebetina has been attributed to acute renal failure (ARF). It is unclear whether the venom components have a direct or indirect action in causing ARF. T...

: The venoms of Tunisian wildlife snakes are complex mixtures containing proteins/ peptides and non-protein molecules. Proteins the most abundant compounds responsible for biological effects venoms. Snake proteins have enzymatic or nonenzymatic activities, which grouped into different families, including C-type lectin proteins, disintegrins (long, medium short disintegrins), Kunitz-type serine ...