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Neurotoxins of Bungarus multicinctus venom. Purification and partial characterization

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00645a031· OSTI ID:7076097
The purification to homogeneity of nine neurotoxic components of the venom of Bungarus multicinctus is described. The purified components include ..cap alpha..-bungarotoxin and two other ..cap alpha..-type synaptic toxins and ..beta..-bungarotoxin and five other ..beta..-type synaptic toxins. The purified toxins have been characterized by electrophoresis, isoelectric focusing, amino acid analysis, and N-terminal amino acid determination. The ..cap alpha..-type synaptic neurotoxins constitute a discrete class with molecular weights of 7000 to 8500, isoelectric points (pI) of 9.0 to 9.2, and N-terminal isoleucine or methionine. The ..beta..-type synaptic neurotoxins constitute a second group with molecular weights of 20,000 to 22,000 and pI = 8.8 to 9.7. Fractions 10 through 13 exhibit a chain structure consisting of a 6000 to 7000 light chain and a 11,000 to 15,000 heavy chain apparently covalently stabilized by interchain disulfides. Fractions 9A and 14 were single chains of 11,000 to 14,000 which resemble the sequenced ..beta..-type synaptic neurotoxin notexin (Halpert, J., and Eaker, D. (1975), J. Biol. Chem. 250, 6990). All of the ..beta..-type synaptic toxins have a single tryptophan and N-terminal aspartic acid or asparagine.
Research Organization:
Lawrence Berkeley Lab., CA
OSTI ID:
7076097
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 16:26; ISSN BICHA
Country of Publication:
United States
Language:
English