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Snake Venom
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 Snakebite, bite, though some species are also able to spit venom. The Venom gland, venom glands that secrete zootoxins are a modification of the parotid gland, parotid salivary glands found in other vertebrates and are usually located on each side of the head, below and behind the eye, and enclosed in a muscular sheath. The venom is stored in large glands called Alveolus, alveoli before being conveyed by a duct to the base of channeled or tubular fangs through which it is ejected. Venom contains more than 20 different compounds, which are mostly proteins and peptides, polypeptides. The complex mixture of proteins, enzymes, and various other substances has toxic and lethal properties. Venom serves to immobilize prey. Enzymes in venom play an important role in the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vipera Berus - Venom Delivery Apparatus
''Vipera'' (; commonly known as the palaearctic vipersspecies:Stephen Spawls, Spawls S, William Roy Branch, Branch B (1995). ''The Dangerous Snakes of Africa: Natural History, Species Directory, Venoms and Snakebite''. Sanibel Island, Florida: Ralph Curtis Books / Dubai: Oriental Press. 192 pp. . and Eurasian vipersspecies:David Mallow, Mallow D, species:David Ludwig, Ludwig D, species:Göran Nilson, Nilson G (2003). ''True Vipers: Natural History and Toxinology of Old World Vipers''. Malabar, Florida: Krieger Publishing Company. 359 pp. ) is a genus of snakes in the subfamily Viperinae of the Family (biology), family Viperidae. The genus has a very wide range, being found from North Africa to just within the Arctic Circle, and from Great Britain to Pacific Asia. The Latin name ''vīpera'' is possibly derived from the Latin (language), Latin words ''vivus'' and ''pario'', meaning "alive" and "bear" or "bring forth"; likely a reference to the fact that most vipers bear live young.Go ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viperidae
Vipers are snakes in the family Viperidae, found in most parts of the world, except for Antarctica, Australia, Hawaii, Madagascar, New Zealand, Ireland, and various other isolated islands. They are venomous snake, venomous and have long (relative to non-vipers), hinged fangs that permit deep envenomation of their prey. Three subfamilies are currently recognized. They are also known as viperids. The name "viper" is derived from the Latin word ''vipera'', -''ae'', also meaning viper, possibly from ''vivus'' ("living") and ''parere'' ("to beget"), referring to the trait viviparity (giving live birth) common in vipers like most of the species of Boidae. The earliest known vipers are believed to have diverged from the rest of the clade Caenophidia in the early Eocene. Description All viperids have a pair of relatively long Solenoglypha#Solenoglyph, solenoglyphous (hollow) fangs that are used to inject venom from glands located towards the rear of the upper jaws, just behind the ey ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cardiotoxin
Cardiotoxicity is the occurrence of heart dysfunction as electric or muscle damage, resulting in heart toxicity. This can cause heart failure, arrhythmia, myocarditis, and cardiomyopathy in patients. Some effects are reversible, while in others, permanent damage requiring further treatment may arise. The heart becomes weaker and is not as efficient in pumping blood. Cardiotoxicity may be caused by chemotherapy (a usual example is the class of anthracyclines) treatment and/or radiotherapy; complications from anorexia nervosa; adverse effects of heavy metals intake; the long-term abuse of or ingestion at high doses of certain strong stimulants such as cocaine; or an incorrectly administered drug such as bupivacaine. Mechanism Many mechanisms have been used to explain cardiotoxicity. While many times, differing etiologies share the same mechanism, it generally depends on the agent inducing cardiac damage. For example, the primary mechanism is thought to be oxidative stress on cardia ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytotoxin
Cytotoxicity is the quality of being toxic Toxicity is the degree to which a chemical substance or a particular mixture of substances can damage an organism. Toxicity can refer to the effect on a whole organism, such as an animal, bacterium, or plant, as well as the effect on a subst ... to cells. Examples of toxic agents are toxic metals, toxic chemicals, microbe neurotoxins, radiation particles and even specific neurotransmitters when the system is out of balance. Also some types of drugs, e.g alcohol (drug), alcohol, and some venom, e.g. from the Bitis arietans, puff adder (''Bitis arietans'') or brown recluse spider (''Loxosceles reclusa'') are toxic to cells. Cell physiology Treating cells with the cytotoxic compound can result in a variety of prognoses. The cells may undergo necrosis, in which they lose membrane integrity and die rapidly as a result of cell lysis. The cells can stop actively growing and dividing (a decrease in cell viability), or the cells can activa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endothelium
The endothelium (: endothelia) is a single layer of squamous endothelial cells that line the interior surface of blood vessels and lymphatic vessels. The endothelium forms an interface between circulating blood or lymph in the lumen and the rest of the vessel wall. Endothelial cells in direct contact with blood are called vascular endothelial cells whereas those in direct contact with lymph are known as lymphatic endothelial cells. Vascular endothelial cells line the entire circulatory system, from the heart to the smallest capillaries. These cells have unique functions that include fluid filtration, such as in the glomerulus of the kidney, blood vessel tone, hemostasis, neutrophil recruitment, and hormone trafficking. Endothelium of the interior surfaces of the heart chambers is called endocardium. An impaired function can lead to serious health issues throughout the body. Structure The endothelium is a thin layer of single flat (squamous) cells that line the inter ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metalloproteinases
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline. Classification There are two subgroups of metalloproteinases: * Exopeptidases, metalloexopeptidases ( EC number: 3.4.17). * Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine Proteases
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. Classification The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile, (S: serine proteases). Substrate specificity Serine prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kallikreins
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by '' KLKB1 gene'') has no known paralogue, while tissue kallikrein-related peptidases (''KLKs'') encode a family of fifteen closely related serine proteases. These genes are localised to chromosome 19q13, forming the largest contiguous cluster of proteases within the human genome. Kallikreins are responsible for the coordination of various physiological functions including blood pressure, semen liquefaction and skin desquamation. Occurrence In 1934, Eugen Werle reported finding a substance in the pancreas of humans and various animals in such large amounts that the pancreas could be taken for its site of origin. He named it kallikrein, by derivation from the Greek word καλλίκρεας (''kallíkreas'') 'pancreas'. Since then, similar enzymes have been found in the biological fluids of humans and other mammals, as well as in some sna ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombin
Prothrombin (coagulation factor II) is encoded in the human by the F2-gene. It is proteolytically cleaved during the clotting process by the prothrombinase enzyme complex to form thrombin. Thrombin (Factor IIa) (, fibrose, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation factor II, E thrombin, beta-thrombin, gamma-thrombin) is a serine protease, that converts fibrinogen into strands of insoluble fibrin, as well as catalyzing many other coagulation-related reactions. History After the description of fibrinogen and fibrin, Alexander Schmidt hypothesised the existence of an enzyme that converts fibrinogen into fibrin in 1872. Prothrombin was discovered by Pekelharing in 1894. Physiology Synthesis Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). The activity of factor Xa is greatly enhanced by binding to activated Factor V (Va), termed the prothrombinase complex. Prothrombin is prod ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phospholipase
A phospholipase is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C, and D, which are distinguished by the type of reaction which they catalyze: *Phospholipase A ** Phospholipase A1 – cleaves the ''sn''-1 acyl chain (where ''sn'' refers to stereospecific numbering). ** Phospholipase A2 – cleaves the ''sn''-2 acyl chain, releasing arachidonic acid. * Phospholipase B – cleaves both ''sn''-1 and ''sn''-2 acyl chains; this enzyme is also known as a lysophospholipase. * Phospholipase C – cleaves before the phosphate, releasing diacylglycerol and a phosphate-containing head group. PLCs play a central role in signal transduction, releasing the second messenger inositol triphosphate. * Phospholipase D – cleaves after the phosphate, releasing phosphatidic acid and an alcohol. Types C and D are considered phosphodiesterases. Endothelial lipase is primarily a phospholipase. Phospho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
