| Literature DB >> 9283 |
G Wunderer, H Fritz, E Wachter, W Machleidt.
Abstract
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.Entities:
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Year: 1976 PMID: 9283 DOI: 10.1111/j.1432-1033.1976.tb10778.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956