Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2007298 | Peptides | 2008 | 9 Pages |
Abstract
Four peptide toxins, SHTX I–III with crab-paralyzing activity and SHTX IV with crab lethality, were isolated from the sea anemone Stichodactyla haddoni and their primary structures elucidated by protein sequencing and cDNA cloning. SHTX I (new toxin, 28 residues), II (analogue of SHTX I, 28 residues) and III (Kunitz-type protease inhibitor, 62 residues) are potassium channel toxins and SHTX IV (48 residues) is a member of the type 2 sea anemone sodium channel toxins. The precursor protein of SHTX IV is composed of a signal peptide, propart and mature peptide, while the propart is missing in that of SHTX III. In addition to these four toxins, an epidermal growth factor-like peptide was detected in S. haddoni by RT-PCR.
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Authors
Tomohiro Honma, Shino Kawahata, Masami Ishida, Hiroshi Nagai, Yuji Nagashima, Kazuo Shiomi,