A polypeptide toxin in the sea anemone Actinia equina homologous with other sea anemone sodium channel toxins: Isolation and amino acid sequence

被引：31

作者：

Lin, XY ^{[1
]}

Ishida, M ^{[1
]}

Nagashima, Y ^{[1
]}

Shiomi, K ^{[1
]}

机构：

[1] TOKYO UNIV FISHERIES,DEPT FOOD SCI & TECHNOL,MINATO KU,KONAN-4,TOKYO 108,JAPAN

来源：

TOXICON | 1996年 / 34卷 / 01期

关键词：

D O I：

10.1016/0041-0101(95)00121-2

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

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.

引用

页码：57 / 65

页数：9

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