2684 Vipoxin Vipoxin is a heterodimeric neurotoxin isolated from the venom of the Bulgarian long-nosed viper or Eastern sand viper (Vipera ammodytes meridionalis). This is the most toxic snake in Europe. Vipoxin represents a noncovalent association of two subunits - a basic and toxic phospholipase A2 enzyme, and an acidic non-enzymatic component (vipoxin's acidic component). The function of the acidic component is to stabilize the neurotoxin's quaternary structure, required for its toxic and enzymatic activities, similarly to the role of the acidic component of crotoxin. The venom has both proteolytic and neurotoxic components and contains hemotoxins with blood coagulant properties, similar to and as powerful as in crotalid venom. Other properties include anticoagulant effects, hemoconcentration and hemorrhage. Bites promote symptoms typical of viperid envenomation, such as pain, swelling and discoloration, all of which may be immediate. There are also reports of dizziness and tingling. Humans respond rapidly to this venom, as do mice and birds. Lizards are less affected, while amphibians may even survive a bite. European snakes, such as Coronella and Natrix, are possibly immune. V. ammodytes venom is used in the production of antivenin for the bite of other European vipers and the snake is farmed for this purpose. 13827.665000000008 Clear solution. >10 mg/mL Injection (sting/bite) (L1814) Vipoxin inhibits the binding of ligands to biogenic amine receptors including dopamine, serotonin and alpha1/alpha2 adrenergic receptors. Vipoxin also exhibits hemolytic and anticoagulant properties. Vipoxin is composed of two subunits - a basic and toxic phospholipase A2 enzyme and an acidic, non-enzymatic component. The phospholipase A2 (PLA2 activity is responsible for the hemolytic properties. Phospholipases are enzymes that release fatty acids from the second carbon group of glycerol. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. The vipoxin LPA2 is also a weakly anticoagulant enzyme. (A15338) Free toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases. LD50: 6.59 mg/kg (Subcutaneous, Mouse) (5) LD50: 0.8 mg/kg (Intravenous, Mouse) (5) LD50: 0.415 mg/kg (Intraperitoneal, Mouse) (5) LD50 of the heterodimer is 0.7-1.2 mg/kg by intraperitoneal injection into mice and 0.9-1.3 mg/kg by intravenous injection into mice. LD50 of the basic component is 10-13 mg/kg by intraperitoneal injection into mice, and 2.2-3.0 mg/kg by intravenous injection into mice, corresponding to 2.4-fold and more than 10-fold the LD50 of the heterodimer, respectively. (A15339) No indication of carcinogenicity to humans (not listed by IARC). Vipoxin is a peptide toxin produced by the Eastern sand viper (Vipera ammodytes meridionalis). (T170) Neurotoxicity, myotoxicity, cardiotoxicity, anticoagulant, convulsant, antiplatelet, hemorrhagic, hemolytic, and edema-inducing effects Bites from snakes in the Viperidae family cause local pain, swelling, edema, skin discoloration, and ecchymosis. (T156) An antivenom exists for viper venom. (L1044) 2009-07-06T21:35:49Z 2014-12-24T20:25:48Z P14420 1AOK true Exogenous Liquid 1aok_bio_r_500.jpg image/jpeg 51318 2014-10-14T18:13:57Z BSEQ0008509