
Neurotoxic proteins from the venom of the banded or formosan krait (bungarus multicinctus, an elapid snake). ... Alpha-bungarotoxin blocks nicotinic acetylcholine receptors and has been used to isolate and study them; beta- and gamma-bungarotoxins act presynaptically causing acetylcholine release and depletion. Both alpha and beta forms have been c...
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Toxins found in the venom of Bungarus multicinctus . a -bungarotoxin: polypeptide toxin (74 residues). A powerful antagonist of acetylcholine it causes virtually irreversible block of the vertebrate neuromuscular junction by binding (as a monomer) to each of the a -subunits of the postsynaptic nicotinic acetycholine receptors (nAChR) Has been much used in identifying, quantifying and localizing these receptors on muscle cells. Will also bind some neuronal nAChR ; b -bungarotoxin: a two-chain phospholipase A2 neurotoxin that acts at the presynaptic site of motor nerve terminals and blocks transmitter release. Subunit A (120 residues) is structurally homologous to other PLA2s, the B subunit (60 residues) has homology with Kunitz-type serine protease inhibitors and dendrotoxins. Binds to subtype of voltage-sensitive potassium channels. k -bungarotoxin: (bungarotoxin 3.1; Toxin F, neuronal bungarotoxin) is a polypeptide (66 residues) from the venom of Bungarus multicinctus . Has considerable homology with a -bungarotoxin. Functional toxin a homodimer. Potent antagonist for a subset of neuronal nAChR but is much less active against muscle receptors.
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Type: Term Pronunciation: bung′gă-rō-tok′sinz Definitions: 1. Constituent proteins of the venom of the southern Asian banded krait Bungarus multicinctus, a snake of the Elapidae family. Used as pharmacologic tools in studying neuromuscular function.
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