The amino acid sequence and position of the free thiol group of a short-chain neurotoxin from common-death-adder ( Acanthophis antarcticus) venom

• Published in: Biochemical Journal
• Main Authors: Kim, H S, Tamiya, N
• Format: Article in Journal/Newspaper
• Language: English
• Published: Portland Press Ltd. 1981
• Subjects: Antarc*; antarcticus
• Online Access: http://dx.doi.org/10.1042/bj1990211; https://portlandpress.com/biochemj/article-pdf/199/1/211/576697/bj1990211.pdf

The amino acid sequence of a short-chain neurotoxin Acanthophis antarcticus c (toxin Aa c) from the venom of an Australian elapid snake, the common death adder (Acanthophis antarcticus, subfamily Acanthophiinae) was elucidated. Toxin Aa c is composed of 62 amino acid residues, including eight half-cystine residues and a cysteine residue. The amino acid sequence of toxin Aa c is homologous with those of other short-chain neurotoxins found in snakes of the family Elapidae, especially with those from snakes of the subfamily Hydrophiinae. The single cysteine residue was located in position 4. Toxin Aa c has a lethal dose (LD50) of 0.08 micrograms/g body weight of mouse on intramuscular injection.