Venom or zootoxin is a type of toxin produced by an animal that is actively delivered through a wound by means of a bite, sting, or similar action. The toxin is delivered through a specially evolved venom apparatus, such as fangs or a stinger, in a process called envenomation. Venom is often distinguished from poison, which is a toxin that is passively delivered by being ingested, inhaled, or absorbed through the skin, and toxungen, which is actively transferred to the external surface of another animal via a physical delivery mechanism.
Snake venom is a highly toxic saliva containing zootoxins that facilitates in the immobilization and digestion of prey. This also provides defense against threats. Snake venom is usually injected by unique fangs during a bite, though some species are also able to spit venom.
Crotalus scutulatus is known commonly as the Mohave Rattlesnake. Other common English names include Mojave Rattlesnake and, referring specifically to the nominate (northern) subspecies: Northern Mohave Rattlesnake and Mojave Green Rattlesnake, the latter name commonly shortened to the more colloquial “Mojave green”. Campbell and Lamar (2004) supported the English name “Mohave (Mojave) rattlesnake” with some reluctance because so little of the snake’s range lies within the Mojave Desert.
Convulxin is a snake venom toxin found in a tropical rattlesnake known as Crotalus durissus terrificus. It belongs to the family of hemotoxins, which destroy red blood cells or, as is the case with convulxin, induce blood coagulation.
Myotoxins are small, basic peptides found in snake venoms and lizard venoms. This involves a non-enzymatic mechanism that leads to severe muscle necrosis. These peptides act very quickly, causing instantaneous paralysis to prevent prey from escaping and eventually death due to diaphragmatic paralysis.
Crotalus concolor, commonly known as the midget faded rattlesnake, faded rattlesnake, and yellow rattlesnake, is a pit viper species found in the western United States. It is a small rattlesnake known for its faded color pattern. Like all other pit vipers, it is venomous.
In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:
BmKAEP is a neurotoxin from the venom of the Manchurian scorpion (Mesobuthus martensii). It is a β-toxin, which shift the activation voltage of sodium channels towards more negative potentials.
Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
CSTX is a name given to a group of closely related neurotoxic peptides present in the venom of the wandering spider Cupiennius salei. There are twenty types so far described for this protein group. However, some are reclassified into cupiennins group of toxin, including CSTX-3, -4, -5, and -6, because of their chemical affinity. The first thirteen were isolated and identified in 1994 by Lucia Kuhn-Nentwig, Johann Schaller, and Wolfgang Nentwig of the Zoological Institute at the University of Bern, Switzerland. The different types are most likely the products of splicing variant of the same gene. They are all L-type calcium channel blockers, and also exhibit cytolytic activity by forming an alpha-helix across the cell membrane in mammalian neurons. They also inhibit voltage-gated calcium channels in insect neurons.
Heteroscopine (HS-1) is the main component of the venom of Heterometrus laoticus. It belongs to the Scorpine toxin family. It is a polypeptide consisting of a defensin-like component on its N-terminal end and a putative potassium channel blocking component on its C-terminal end. It has antimicrobial effect on some bacteria, but not on fungi.
Tamulotoxin is a venomous neurotoxin from the Indian Red Scorpion.
Venom in snakes and some lizards is a form of saliva that has been modified into venom over its evolutionary history. In snakes, venom has evolved to kill or subdue prey, as well as to perform other diet-related functions. While snakes occasionally use their venom in self defense, this is not believed to have had a strong effect on venom evolution. The evolution of venom is thought to be responsible for the enormous expansion of snakes across the globe.
Kaliseptine (AsKS) is a neurotoxin which can be found in the snakelocks anemone Anemonia viridis. It belongs to a class of sea anemone neurotoxins that inhibits voltage-gated potassium channels.
Three-finger proteins or three-finger protein domains are a protein superfamily consisting of small, roughly 60-80 amino acid residue protein domains with a common tertiary structure: three beta strand loops extended from a hydrophobic core stabilized by disulfide bonds. The family is named for the outstretched "fingers" of the three loops. Members of the family have no enzymatic activity, but are capable of forming protein-protein interactions with high specificity and affinity. The founding members of the family, also the best characterized by structure, are the three-finger toxins found in snake venom, which have a variety of pharmacological effects, most typically by disruption of cholinergic signaling. The family is also represented in non-toxic proteins, which have a wide taxonomic distribution; 3FP domains occur in the extracellular domains of some cell-surface receptors as well as in GPI-anchored and secreted globular proteins, usually involved in signaling.
Crotoxin (CTX) is the main toxic compound in the snake venom of the South American rattlesnake, Crotalus durissus terrificus. Crotoxin is a heterodimeric beta-neurotoxin, composed of an acidic, non-toxic and non-enzymatic subunit (CA), and a basic, weakly toxic, phospholipase A2 protein (CB). This neurotoxin causes paralysis by both pre- and postsynaptic blocking of acetylcholine signalling.
U7-ctenitoxin-Pn1a (or U7-CNTX-Pn1a for short) is a neurotoxin that blocks TRPV1 channels, and can exhibit analgestic effects. It is naturally found in the venom of Phoneutria nigriventer.
κ-KTx2.5 is a toxin found in the venom of the scorpion, Opisthacanthuscayaporum. The toxin belongs to the κ-KTx family, a channel blocker family that targets voltage-gated potassium channels (Kv) 1.1 and 1.4.
Crotalus durissus cumanensis is a subspecies of venomous pit viper from Colombia and Venezuela. They account for 1-3% of all snake bites in Colombia.
