@article{ref1,
title="A polypeptide toxin in the sea anemone Actinia equina homologous with other sea anemone sodium channel toxins: isolation and amino acid sequence",
journal="Toxicon: Journal of the International Society on Toxinology",
year="1996",
author="Lin, X. Y. and Ishida, M. and Nagashima, Y. and Shiomi, K.",
volume="34",
number="1",
pages="57-65",
abstract="The sea anemone (Actinia equina) was newly established to contain a polypeptide toxin (named Ae I) having lethal activity to crabs, besides the well-known cytolytic toxins (equinatoxins) of proteinic nature. Ae I, with a minimum lethal dose against crabs of 25 micrograms/kg, was easily isolated by gel filtration on Sephadex G-50 and reverse-phase HPLC on Nucleosil 300-7C18. Its amino acid composition is characterized by the abundance of Gly, the absence of Ala and the presence of Met. The complete amino acid sequence of Ae I was determined. Ae I has high sequence homology with type 1 sea anemone neurotoxins. Interestingly, the polypeptide chain of Ae I comprises 54 amino acid residues, being 5-8 residues longer than the known type 1 toxins having 46-49 residues.<p /><p>Language: en</p>",
language="en",
issn="0041-0101",
doi="",
url="http://dx.doi.org/"
}