Isolation and primary structure of the major toxin from sea snake, Acalyptophis peronii, venom.
The major neurotoxin from the venom of Acalyptophis peronii captured in the Gulf of Thailand was isolated. Although there are two toxic fractions in the venom, the most toxic and abundant fraction was selected for purification and chemical characterization. The LD50 of the major toxin is 0.125 micrograms/g mice, indicating an extremely toxic nature. The toxin consists of 60 amino acid residues with methionine as the amino-terminal and asparagine as the carboxy-terminal end. It contains nine half-cystine residues. There is 1 mol each of tryptophan, tyrosine, methionine, valine, aspartic acid, leucine, and alanine, and there is no phenylalanine. The molecular weight calculated from the amino acid sequence determination was 6600. The toxin replaces alpha-bungarotoxin in binding with the acetylcholine receptor, indicating that the A. peronii major neurotoxin competes with alpha-bungarotoxin for the same binding site of the acetylcholine receptor.
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Department of Biochemistry, Colorado State University, Fort Collins 80523.
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D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D002038:Bungarotoxins / Q000378:metabolism; D004546:Elapid Venoms / Q000032:analysis* / Q000302:isolation & purification* / Q000378:metabolism; D007928:Lethal Dose 50; D051379:Mice; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D011950:Receptors, Cholinergic / Q000032:analysis; D030162:Reptilian Proteins
C054654:Acalyptophis neurotoxin; D002038:Bungarotoxins; D004546:Elapid Venoms; D009498:Neurotoxins; D011950:Receptors, Cholinergic; D030162:Reptilian Proteins