Chemistry
Charles Lucien Bonaparte, the son of Lucien Bonaparte, younger brother of Napoleon Bonaparte, was the first to establish the proteinaceous nature of snake venom in 1843.
Proteins constitute 90-95% of venom's dry weight and they are responsible for almost all of its biological effects. Among hundreds, even thousands of proteins found in venom, there are toxins, neurotoxins in particular, as well as nontoxic proteins (which also have pharmacological properties), and many enzymes, especially hydrolytic ones. Enzymes (molecular weight 13-150 KDa) make-up 80-90% of viperid and 25-70% of elapid venoms: digestive hydrolases, L-amino acid oxidase, phospholipases, thrombin-like pro-coagulant, and kallikrein-like serine proteases and metalloproteinases (hemorrhagins), which damage vascular endothelium. Polypeptide toxins (molecular weight 5-10 KDa) include cytotoxins, cardiotoxins, and postsynaptic neurotoxins (such as α-bungarotoxin and α-Cobratoxin), which bind to acetylcholine receptors at neuromuscular junctions. Compounds with low molecular weight (up to 1.5 KDa) include metals, peptides, lipids, nucleosides, carbohydrates, amines, and oligopeptides, which inhibit angiotensin converting enzyme (ACE) and potentiate bradykinin (BPP). Inter- and intra-species variation in venom chemical composition is geographical and ontogenic. Phosphodiesterases interfere with the prey's cardiac system, mainly to lower the blood pressure. Phospholipase A2 causes hemolysis by lysing the phospholipid cell membranes of red blood cells. Amino acid oxidases and proteases are used for digestion. Amino acid oxidase also triggers some other enzymes and is responsible for the yellow colour of the venom of some species. Hyaluronidase increases tissue permeability to accelerate absorption of other enzymes into tissues. Some snake venoms carry fasciculins, like the mambas (Dendroaspis), which inhibit cholinesterase to make the prey lose muscle control.
Type | Name | Origin |
Oxydoreductases | dehydrogenase lactate | Elapidae |
L-amino-acid oxidase | All species | |
Catalase | All species | |
Transferases | Alanine amino transferase | |
Hydrolases | Phospholipase A2 | All species |
Lysophospholipase | Elapidae, Viperidae | |
Acetylcholinesterase | Elapidae | |
Alkaline phosphatase | Bothrops atrox | |
Acid phosphatase | Deinagkistrodon acutus | |
5'-Nucleotidase | All species | |
Phosphodiesterase | All species | |
Deoxyribonuclease | All species | |
Ribonuclease 1 | All species | |
Adenosine triphosphatase | All species | |
Amylase | All species | |
Hyaluronidase | All species | |
NAD-Nucleotidase | All species | |
Kininogenase | Viperidae | |
Factor-X activator | Viperidae, Crotalinae | |
Heparinase | Crotalinae | |
α-Fibrinogenase | Viperidae, Crotalinae | |
β-Fibrinogenase | Viperidae, Crotalinae | |
α-β-Fibrinogenase | Bitis gabonica | |
Fibrinolytic enzyme | Crotalinae | |
Prothrombin activator | Crotalinae | |
Collagenase | Viperidae | |
Elastase | Viperidae | |
Lyases | Glucosamine ammonium lyase |
Snake toxins vary greatly in their functions. Two major classifications of toxins found in snake venoms include neurotoxins (mostly found in elapids) and hemotoxins (mostly found in viperids). However, there are exceptions - an African spitting cobra Naja nigricollis's venom consists mainly of hemotoxins, while the Mojave rattlesnake's venom is primarily neurotoxic. However, there are numerous other different types of toxins which both elapids or viperids may carry.
α-neurotoxins | α-Bungarotoxin, α-toxin, erabutoxin, cobratoxin |
---|---|
β-neurotoxins | Notexin, ammodytoxin, β-Bungarotoxin, crotoxin, taipoxin |
κ-Toxins | κ-Toxin |
Dendrotoxins | Dendrotoxin, toxins I and K |
Cardiotoxins | y-Toxin, cardiotoxin, cytotoxin |
Myotoxins | Myotoxin-a, crotamine |
Sarafotoxins | Sarafotoxins a, b, and c |
Hemorrhagins | Phospholipase A2, mucrotoxin A, hemorrhagic toxins a, b, c..., HT1, HT2 |
Read more about this topic: Snake Venom
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