Lin X Y, Ishida M, Nagashima Y, Shiomi K
Department of Food Science and Technology, Tokyo University of Fisheries, Japan.
Toxicon. 1996 Jan;34(1):57-65. doi: 10.1016/0041-0101(95)00121-2.
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.
海葵（Actinia equina）最近被发现除了含有众所周知的蛋白质性质的细胞溶解毒素（海葵毒素）外，还含有一种对螃蟹具有致死活性的多肽毒素（命名为Ae I）。Ae I对螃蟹的最小致死剂量为25微克/千克，通过在Sephadex G - 50上进行凝胶过滤和在Nucleosil 300 - 7C18上进行反相高效液相色谱法很容易分离出来。其氨基酸组成的特点是甘氨酸含量丰富，不含丙氨酸且含有甲硫氨酸。确定了Ae I的完整氨基酸序列。Ae I与1型海葵神经毒素具有高度的序列同源性。有趣的是，Ae I的多肽链由54个氨基酸残基组成，比已知的含有46 - 49个残基的1型毒素长5 - 8个残基。
