Snake Venom Research Paper

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More than 2,500 species of snakes exists and of which 600 are known to produce venom. Venom is a secretion of snakes and other organisms, which are secreted by a gland in their body called venom gland. The venom constitutes of enzymatic proteins such as phospholipase A2 (PLA2), phosphodiesterase, phosphomonoesterase, L-amino acid oxidase, nucleases, specific endopeptidases, and nonspecific endopeptidases and non-enzymatic proteins which include Nerve growth factor like, Vascular Endothelial Growth Factor like and Cysatin.[5] The components and activity of these enzymes are important with respect to the mode of action and the targets of the venom.
Snake venoms vary in composition. They generally contain multiple proteins serving a wide range of functions. There are about 28 protein families which have been isolated from venom of different snake species and from which 12 are found in all species.[5] The components of venom are known to vary
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Snake venom nucleases are classified as endonucleases and exonucleases. Endonucleases include DNases, which specifically hydrolyze DNA, and RNases, which specifically hydrolyze RNA. Exonucleases include phosphodiesterases (PDE), which hydrolyze both DNA and RNA. An endonuclease activity in snake venom was first reported in 1919.[1]
These nucleases isolated from the snake venom, namely Dnase, Rnases and phosphodiesterases endogenously liberate purines, which act as multitoxins. A DNase activity with pH optimum of 5.0 was purified from Bothrops atrox venom. A specific ribonuclease was isolated from the venom of Naja oxiana hydrolyzing double stranded RNA and produced oligonucleotides of 2-4 bases. This had an apparent molecular mass of ~14 to 16 kDa.[1] Phosphodiesterases catalyze the hydrolysis of phosphodiester bonds at basic pH and Crotalid and viperid venoms have been shown to contain higher activity of

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