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Purification and properties of a myotoxin from Conus geographus venom
Authors:Lourdes J Cruz  William R Gray  Baldomero M Olivera
Institution:1. Department of Biochemistry, College of Medicine, University of the Philippines, Manila, Philippines;2. Department of Biology, University of Utah, Salt Lake City, Utah 84112 USA
Abstract:Previous studies (R. Endean et al. (1974), Toxicon12: 131–138) indicate that whole venom from the marine mollusc Conus geographus directly inhibits skeletal muscle, leaving peripheral nerves, cardiac and smooth muscle unaffected. A quantitative bioassay has been used to detect and measure biologically active myotoxin. By using chromatography on phosphocellulose, purified myotoxin is obtained which has the same physiological effects as whole venom. The LD50 of purified toxin is 12 μg/kg in mice, death occurring as a result of flaccid paralysis and respiratory failure. A biochemical characterization of the purified myotoxin indicates that it is a peptide of 13 amino acids containing two disulfide bonds. This and related peptide myotoxins from Conus should be of exceptional interest in muscle physiology.
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