Characterization of polypeptide neurotoxins from the venom of Bungarus caeruleus |
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Authors: | Terry W. Moody Michael A. Raftery |
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Affiliation: | Church Laboratory of Chemical Biology, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125 USA |
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Abstract: | The venom of the krait Bungarus caeruleus has been fractionated into several components. Two of the basic components were highly toxic to mice and had significant levels of phospholipase A activity. These components appear to be similar in their action to the presynaptic neurotoxin β-bungarotoxin. Two other components were toxic to mice and also reduced the rate of α-bungarotoxin binding to the purified acetylcholine receptor: These components appear to be postsynaptic neurotoxins similar to α-bungarotoxin. Two acidic components displayed A-type phospholipase activity and perturbed the carbamylcholine binding properties of acetylcholine receptor-rich membrane preparations. |
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