Triflin
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Triflin
Triflin is a cysteine-rich secretory protein (CRISP), which is excreted by the venom gland of the Habu snake (''Trimeresurus flavoviridis''). Triflin reduces high potassium-induced smooth muscle contraction, suggesting a blocking effect on L-type calcium channels. Sources Triflin is a toxin derived from snake venom. The toxin is produced in the gland of the Habu snake, ''Trimeresurus flavoviridis''. Chemistry Triflin is a cysteine-rich secretory protein, which means it belongs to the CRISP family. This is a group of single chain polypeptides found in various organisms. Triflin weighs 25 kDa and consists of 221 amino-acid residues. The first 163 residues of the N-terminal domain forms an α-β-α sandwich core. This domain is comparable with group 1 plant pathogenesis-related protein (PR-1). The C-terminal domain, has five disulfide bridges. This domain is responsible for the selectivity of the protein and consists of two subdomains: N-terminal subdomain (Cys 167 to Cys 179) a ...
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Ophanin
Ophanin is a toxin found in the venom of the King Cobra (''Ophiophagus hannah''), which lives throughout South East Asia. This toxin belongs to the cysteine-rich secretory protein (CRISP) family. Ophanin weakly blocks the contraction of smooth muscles elicited by high potassium-induced depolarization, suggesting that it inhibits voltage-dependent calcium channels. Etymology The toxin was named ''ophanin'' after the snake whose venom it is derived from, the King Cobra (''Ophiophagus hannah''). Sources Ophanin is produced in the venom glands of the King Cobra (''O. Hannah''). Although the venom has relatively low toxicity, this is compensated by the high amounts of it injected into the prey for each bite. Chemistry Structure Ophanin was successfully isolated from ''O. Hannah'' venom by gel filtration and cation-exchange chromatography. Its molecular weight is 25 kDa (from positions 19 – 239), which conforms to the molecular mass predicted from its cDNA sequences. Hom ...
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Cysteine-rich Secretory Protein
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. Structure CRISPs contain two domains joined by a hinge region. The larger domain is a CAP-like 'Pathogenesis-related 1' domain (PR-1), followed by the smaller ShK-like 'Cysteine-Rich Domain' (CRD). CRISPs are glycoproteins, with a number of carbohydrate glycans covalently attached to amino acid side-chains on their surface via glycosylation. The primary structure is also rich in cysteine that form disulfide bonds, particularly in the hinge region and CRD. Mammalian reproduction CRISPs are found in the testes and epidid ...
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Ablomin
Ablomin is a toxin present in the venom of the Japanese Mamushi snake, which blocks L-type voltage-gated calcium channels. Etymology The protein ablomin is a component of the venom of the Japanese Mamushi snake, ''Gloydius blomhoffii''. The term ‘ablomin’ is an acronym derived from ''Agkistrodon blomhoffi'', an old name for this snake. Sources The protein can be found in the venom of the Japanese Mamushi snake, a member of the Viperidae family. Chemistry Ablomin is part of the Cystein-Rich Secretory Protein (CRISP) family. CRISPs comprise a particular group of snake venom proteins distributed among the venom of several families of snakes, such as elapids, colubrids and vipers. The protein exists of 240 amino acids, coded by an mRNA of 1336 base pairs. Structurally, it is composed of three distinct regions: an N-terminal protein domain, a hinge region and a C-terminal cystein-rich domain. It has a molecular mass of 25 kDa The dalton or unified atomic mass unit (sy ...
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Latisemin
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. Sources Latisemin is a component of the venom produced by the Erabu sea snake (''Laticauda semifasciata'') of the family Elapidae and the Laticauda genus. These sea snakes inhabit coral reef areas in the seas of Southern Japan, Southeast Asia, and Australia. Though highly venomous, this snake is comparatively unaggressive, and is in fact caught and eaten in Erabu soup in Japan. Biochemistry Latisemin has a molecular weight of 24 kDa and consists of 217 amino acids. It belongs to the CRISP (cysteine-rich secretory protein) glycoprotein subfamily, which are single chain polypeptides containing strictly conserved cysteines (cysteines not oxidised to c ...
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Piscivorin
Piscivorin is a component of snake venom secreted by the Eastern Cottonmouth (''Agkistrodon piscivorus piscivorus''). It is a member of the cysteine-rich secretory protein (CRISP) family, which blocks voltage-dependent calcium channels. Etymology The name of piscivorin comes from the snake species name piscivorus, which is derived from the Latin words ''pisces'' and ''vorare'', meaning 'fish' and 'to devour' respectively. Sources Piscivorin is produced in the venom glands of the Eastern Cottonmouth snake (''Agkistrodon piscivorus piscivorus''), which populates the Eastern United States. Typically, crude venom from the Eastern Cottonmouth contains approximately 1.25% of piscivorin. Biochemistry Piscivorin belongs to the cysteine-rich secretory protein (CRISP) family, which are secreted as single-chain proteins with molecular masses between 20 and 30 kDa. They display significant amino acid sequence homology. Sixteen cysteine residues, forming 8 disulfide bonds, are strictly ...
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Venom
Venom or zootoxin is a type of toxin produced by an animal that is actively delivered through a wound by means of a bite, sting, or similar action. The toxin is delivered through a specially evolved ''venom apparatus'', such as fangs or a stinger, in a process called envenomation. Venom is often distinguished from poison, which is a toxin that is passively delivered by being ingested, inhaled, or absorbed through the skin, and toxungen, which is actively transferred to the external surface of another animal via a physical delivery mechanism. Venom has evolved in terrestrial and marine environments and in a wide variety of animals: both predators and prey, and both vertebrates and invertebrates. Venoms kill through the action of at least four major classes of toxin, namely necrotoxins and cytotoxins, which kill cells; neurotoxins, which affect nervous systems; myotoxins, which damage muscles; and haemotoxins, which disrupt blood clotting. Venomous animals cause tens of thousa ...
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Trimeresurus Flavoviridis
''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,Gumprecht A, Tillack F, , Captain A, Ryabov S. 2004. ''Asian Pitvipers''. GeitjeBooks. Berlin. 1st Edition. 368 pp. . Okinawa habu,U.S. Navy. 1991. ''Poisonous Snakes of the World''. US Govt. New York: Dover Publications Inc. 203 pp. . and Kume Shima habu.Mehrtens JM. 1987. ''Living Snakes of the World in Color''. New York: Sterling Publishers. 480 pp. .'' Description Growing to an average total length of , with a maximum of , this is the largest member of its genus. It is slenderly built and gracefully proportioned with a large head. The crown of the head is covered with small scales. ''P. flavorviridis'' has a light olive or brown ground color, overlaid with elongated dark green or brownish blotches. The blotches have yellow edges, sometimes contain yellow spots, and frequently fuse to produce wavy str ...
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L-type Calcium Channel
The L-type calcium channel (also known as the dihydropyridine channel, or DHP channel) is part of the high-voltage activated family of voltage-dependent calcium channel. "L" stands for long-lasting referring to the length of activation. This channel has four isoforms: Cav1.1, Cav1.2, Cav1.3, and Cav1.4. L-type calcium channels are responsible for the excitation-contraction coupling of skeletal, smooth, cardiac muscle, and for aldosterone secretion in endocrine cells of the adrenal cortex. They are also found in neurons, and with the help of L-type calcium channels in endocrine cells, they regulate neurohormones and neurotransmitters. They have also been seen to play a role in gene expression, mRNA stability, neuronal survival, ischemic-induced axonal injury, synaptic efficacy, and both activation and deactivation of other ion channels. In cardiac myocytes, the L-type calcium channel passes inward Ca2+ current (ICaL) and triggers calcium release from the sarcoplasmic reticul ...
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Amino Acids
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling lif ...
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N-terminal
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that j ...
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Pathogenesis-related Protein
Pathogenesis-related (PR) proteins are proteins produced in plants in the event of a pathogen attack. They are induced as part of systemic acquired resistance. Infections activate genes that produce PR proteins. Some of these proteins are antimicrobial, attacking molecules in the cell wall of a bacterium or fungus. Others may function as signals that spread “news” of the infection to nearby cells. Infections also stimulate the cross-linking of molecules in the cell wall and the deposition of lignin, responses that set up a local barricade that slows spread of the pathogen to other parts of the plant. Salicylic acid plays a role in the resistance to pathogens by inducing the production of pathogenesis-related proteins. Many proteins found in wine are grape pathogen-related proteins. Those include thaumatin-like proteins and chitinases. Many pathogenesis-related protein families also coincide with groups of human allergens, even though the allergy may have nothing to do with th ...
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