A polypeptide toxin in the sea anemone Actinia equina homologous with other sea anemone sodium channel toxins: Isolation and amino acid sequence
A polypeptide toxin in the sea anemone Actinia equina homologous with other sea anemone sodium channel toxins: Isolation and amino acid sequence
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DOI：
10.1016/0041-0101(95)00121-2
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发表时间：
1996-01-01
期刊：
影响因子：
2.8
通讯作者：
Shiomi, K
中科院分区：
文献类型：
--
作者：
Lin, XY;Ishida, M;Shiomi, K
海葵（Actininequina）是新近发现的一种多肽毒素（命名为AeI），除已知的具有蛋白质性质的细胞溶解毒素（Equinatoxins）外，还对螃蟹具有致死活性。Ae I对螃蟹的最小致死剂量为25 μ g/kg，通过Sephadex G-50凝胶过滤和Nucleosil 300- 7 C18反相H-PLC容易地分离。其氨基酸组成的特点是丰富的甘氨酸，丙氨酸的情况下，蛋氨酸的存在。测定了Ae Ⅰ的全氨基酸序列。Ae I与1型海葵神经毒素具有很高的序列同源性。有趣的是，Ae I的多肽链包含54个氨基酸残基，比已知的具有46-49个残基的1型毒素长5-8个残基。
The sea anemone (Actinin 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 mu g/kg, was easily isolated by gel filtration on Sephadex G-50 and reverse-phase H-PLC 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.