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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 injected by unique fangs during a bite, whereas some species are also able to spit venom.
Trimeresurus is a genus of venomous pit vipers found in Asia from the Indian Subcontinent throughout Southeast Asia, China, and the Pacific Islands. Currently 44 species are recognized. Common names include Asian palm pit vipers, Asian lanceheads, and green pit vipers.
Gloydius blomhoffii, commonly known as the mamushi, Japanese moccasin, Japanese pit viper, Qichun snake, Salmusa or Japanese mamushi, is a venomous pit viper species found in Japan. It was once considered to have 4 subspecies, but it is now considered monotypic.
Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction
Habushu (ハブ酒) is an awamori-based liqueur made in Okinawa, Japan. Other common names include Habu Sake or Okinawan Snake Wine. Habushu is named after the habu snake, Trimeresurus flavoviridis, which belongs to the pit viper subfamily of vipers, and is closely related to the rattlesnake and copperhead. Like all vipers, Habu snakes are venomous. These snakes are native to parts of Southeast Asia, including large island groups such as the Philippines, Ryukyus, and Japan.
Ovophis okinavensis, commonly known as the hime habu (ヒメハブ), Ryukyu Island pit viper, and the Okinawan pitviper, is a venomous pitviper species found in the Ryukyu Islands of Japan. No subspecies are currently recognized.
Protobothrops flavoviridis is a species of venomous pit viper endemic to the Ryukyu Islands of Japan. No subspecies are currently recognized. Local common names include habu, Okinawa habu, and Kume Shima habu.
Trimeresurus gracilis, commonly known as the Taiwan pit viper or Taiwan mountain pitviper, is a venomous pit viper species endemic to Taiwan. No subspecies are currently recognized. The species is known as kikushi habu in Japanese.
Triflin is a cysteine-rich secretory protein (CRISP), which is excreted by the venom gland of the Habu snake. Triflin reduces high potassium-induced smooth muscle contraction, suggesting a blocking effect on L-type calcium channels.
Latisemin is a cysteine-rich secretory protein that can be isolated from the venom of the Black-banded sea krait, a sea snake indigenous to the warmer waters of the western Pacific Ocean. It is a toxin that inhibits cyclic nucleotide-gated ion channels and blocks L-type calcium channels, thereby reducing smooth muscle contraction.
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins. They are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily and also contain a domain related to the ShK toxins. They are substantially implicated in the functioning of the mammalian reproductive system. CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.
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.
Leucolysin is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Horrilysin 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
Mucrolysin 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
- ↑ Takahashi T, Ohsaka A (February 1970). "Purification and characterization of a proteinase in the venom of Trimeresurus flavoviridis. Complete separation of the enzyme from hemorrhagic activity". Biochimica et Biophysica Acta (BBA) - Enzymology. 198 (2): 293–307. doi:10.1016/0005-2744(70)90062-8. PMID 4984550.
- ↑ Takeya H, Arakawa M, Miyata T, Iwanaga S, Omori-Satoh T (July 1989). "Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis". Journal of Biochemistry. 106 (1): 151–7. doi:10.1093/oxfordjournals.jbchem.a122805. PMID 2777746.
