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

Abstract

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.

• Authors: H S Kim, N Tamiya
• Journal: The Biochemical journal (Biochem J) Vol. 199 Issue 1 Pg. 211-8 (Oct 01 1981) ISSN: 0264-6021 [Print] England
• PMID: 7337702 (Publication Type: Journal Article)

Chemical References

• Elapid Venoms
• Neurotoxins
• Peptide Fragments
• Sulfhydryl Compounds
• Acanthophis antarcticus toxin Aa c

Topics

• Amino Acid Sequence
• Animals
• Elapid Venoms (isolation & purification, metabolism)
• Lethal Dose 50
• Neurotoxins (metabolism)
• Peptide Fragments (analysis)
• Sulfhydryl Compounds (analysis)