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Crotalus is a genus of venomous pit vipers in the family Viperidae, commonly known as rattlesnakes or rattlers. The genus is found only in the Americas from southern Canada to northern Argentina. The generic name Crotalus is derived from the Greek word κρόταλονkrótalοn, which means "rattle" or "castanet", and refers to the rattle on the end of the tail, which makes this group so distinctive. As of July 2023, 44 to 53 species are recognized as being valid.
The timber rattlesnake, canebrake rattlesnake, or banded rattlesnake is a species of pit viper endemic to eastern North America. Like all other pit vipers, it is venomous, with a very toxic bite. C. horridus is the only rattlesnake species in most of the populous Northeastern United States and is second only to its relatives to the west, the prairie rattlesnake, as the most northerly distributed venomous snake in North America. No subspecies are currently recognized.
Disintegrins are a family of small proteins from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion.
The eastern diamondback rattlesnake is a species of pit viper in the family Viperidae. The species is endemic to the Southeastern United States. It is one of the heaviest venomous snakes in the Americas and the largest rattlesnake. No subspecies are recognized.
The western diamondback rattlesnake or Texas diamond-back is a rattlesnake species and member of the viper family, found in the southwestern United States and Mexico. Like all other rattlesnakes and all other vipers, it is venomous. It is likely responsible for the majority of snakebite fatalities in northern Mexico and the greatest number of snakebites in the U.S. No subspecies are currently recognized.
Pepsin A is an enzyme. This enzyme catalyses the following chemical reaction
Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction
Endothiapepsin is an enzyme. This enzyme catalyses the following chemical reaction
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 B is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Atroxase is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin E is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin F is an enzyme. This enzyme catalyses the following chemical reaction
Ruberlysin is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction
Fibrolase is an enzyme. This enzyme catalyses the following chemical reaction
Jararhagin is an enzyme. This enzyme catalyses the following chemical reaction
References
- ↑ Civello DJ, Duong HL, Geren CR (February 1983). "Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom". Biochemistry. 22 (4): 749–55. doi:10.1021/bi00273a007. PMID 6340728.
- ↑ Civello DJ, Moran JB, Geren CR (February 1983). "Substrate specificity of a hemorrhagic proteinase from timber rattlesnake venom". Biochemistry. 22 (4): 755–62. doi:10.1021/bi00273a008. PMID 6340729.
