Wunderer G, Fritz H, Wachter E, Machleidt W
Eur J Biochem. 1976 Sep;68(1):193-8. doi: 10.1111/j.1432-1033.1976.tb10778.x.
Toxin II from Anemonia sulcata, the main component of the sea anemone venom, consists of 47 amino acid residues which are interconnected by three disulfide bridges. The S-aminoethylated polypeptide was coupled to activated glass beads and sequenced to position 33 by automated solid-phase Edman degradation. Blanks arising from anchor points and the rest of the sequence were determined from tryptic peptides of the [14C]carboxymethylated toxin. Toxin II shows no significant homologies with other known sequences of neurotoxins or cardiotoxins. It might constitute a new class of polypeptide toxins.
来自沟迎风海葵的毒素II是海葵毒液的主要成分,由47个氨基酸残基组成,这些残基通过三个二硫键相互连接。将S-氨乙基化多肽与活化的玻璃珠偶联,并通过自动固相埃德曼降解法测序至第33位。由锚定点和序列其余部分产生的空白由[14C]羧甲基化毒素的胰蛋白酶肽段确定。毒素II与其他已知的神经毒素或心脏毒素序列没有显著同源性。它可能构成一类新的多肽毒素。