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King Cobra Venom ( Ophiophagus Hannah Snake) is a very venomous and dangerous snake which is widely distributed in India, China, Malaysia, Indonesia, Southeast Asia, and as far as the Philippines.
King Cobra Venom ( Ophiophagus Hannah Snake) is the largest venomous snake in the world, and can inject an extremely large quantity of venom in one bite. Envenomation signifies a true medical emergency. In this particular species, envenomation usually presents predominately with systemic neurologic manifestations. Drowsiness, neurological and neuromuscular symptoms may develop early; paralysis, ventilatory failure or death often ensue rapidly.
King Cobra ( Ophiophagus Hannah Snake) was found to actively interfere in hemostatic stages such as fibrin clot formation, platelet activation/aggregation, and fibrin clot dissolution. It decreased partial thromboplastin time (aPTT), prothrombin time (PT), and thrombin clotting time (TCT).
King Cobra ( Ophiophagus Hannah Snake) L-amino acid oxidase (LAAO), a heat-stable enzyme, is an extremely potent antiproliferative agent against cancer cells when compared with LAAO isolated from other snake venoms.
King Cobra Venom ( Ophiophagus Hannah Snake), also known as the hamadryad, is a venomous snake species in the family Elapidae, endemic to forests from India through Southeast Asia.
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The king cobra (Ophiophagus hannah) is the only member of its genus. “The king cobra is the longest species of venomous snake in the world,” said Viernum. Though there are other snakes with more potent venom, the amount of neurotoxin that a king cobra can emit in one bite is enough to kill 20 people — or one elephant Viper venom is known to prevent blood from clotting, which is useful for anticoagulant drugs. Venomous marine snails: Venom from the cone snail was used to make the drug ziconotide, which is used to treat chronic pain. … King Cobra: A specific toxin in King Cobra venom shows promise for treating chronic pain.
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Our team of researchers reveals a detailed account of the proteins in the venom of king cobras. Snake venoms always have intrigued scientists, because they “have a rich diversity of biological activities. Among other things, venoms contain various proteases, lipases, nerve-growth factors and enzyme inhibitors. Besides understanding how venoms function, researchers want to develop better antidotes to snake venom and identify molecules from venom that can be exploited as drugs, such as painkillers, anticlotting medications and blood pressure treatments. Domont points to captopril, a drug now commonly used to treat high blood pressure and heart failure. It was derived from a molecule found in the venom of a poisonous Brazilian viper. We are the best suppliers of venoms of all types at moderate prices.we also offer a fast and safe shipping to all clients. We also have scorpion venoms for sale now at cheap prices with discreet packaging and over night shipping worldwide.
We are the most reliable and largest producers and suppliers of snake venoms in the USA, Europe, Asia with the biggest venom bank with 98% purity. Our snakes are kept in enclosures exclusively designed to accommodate our climate and are fed a well balanced to varied diet of rats, mice frogs and quail. Snake venom is highly modified saliva containing zootoxins which facilitates the immobilization and digestion of prey, and defense against threats. It is injected by unique fangs after a bite, and some species are also able to spit their venom.
Seven milliliters of a king cobra’s venom can kill 20 people. But what exactly is in the snake’s venom? Researchers have pursued that question for decades.
Now, in a paper published in the journal Molecular & Cellular Proteomics, a team of researchers reveals a detailed account of the proteins in the venom of king cobras. “I believe this study to be one of the most complete and precise catalogues of proteins in a venom yet obtained,” states Neil Kelleher at Northwestern University, one of the study’s senior investigators.
Snake venoms always have intrigued scientists, because they “have a rich diversity of biological activities,” says Kelleher’s collaborator Gilberto Domont at Universidade Federal do Rio de Janeiro in Brazil. Among other things, venoms contain various proteases, lipases, nerve-growth factors and enzyme inhibitors. Besides understanding how venoms function, researchers want to develop better antidotes to snake venom and identify molecules from venom that can be exploited as drugs, such as painkillers, anticlotting medications and blood pressure treatments. Domont points to captopril, a drug now commonly used to treat high blood pressure and heart failure. It was derived from a molecule found in the venom of a poisonous Brazilian viper.
Although the venom of the king cobra, the largest venomous snake in the world, which can stretch up to 13 feet, has been analyzed previously, questions persist about the venom. How do the sequences of the toxins evolutionarily vary? How do some post-translational modifications on proteins make the venom lethal? But to answer these questions, researchers need a proper count of the proteins in king cobra venom.
The advent of proteomics has allowed scientists to survey the rich diversity of proteins in a given sample. There are different approaches that rely on mass spectrometry to carry out proteomic analyses. One approach is called top-down proteomics. It allows researchers to look at proteins as whole, intact entities. In the more conventional approach, called bottom-up proteomics, proteins are cut into bite-sized fragments for analysis.
In bottom-up proteomics, researchers have to use computer algorithms to stitch back together protein fragments identified by mass spectrometry. Top-down proteomics avoids this problem. Its biggest advantage is that it can capture variations within the proteins as well as post-translational modifications.
Kelleher’s group is one of the leaders in developing top-down proteomics, so that’s what the investigators decided to use to analyze king cobra venom. Domont, Kelleher, Domont’s graduate student, Rafael Melani, and colleagues obtained venom from two Malaysian king cobras held at the Kentucky Reptile Zoo. They analyzed the venom by top-down proteomics in two modes, denatured and native. In the denatured mode, the protein complexes were taken apart; in the native mode, the venom was kept as is so the protein complexes remained intact.