Abstract
A novel neuropeptide with a relaxing activity on the dorsal retractor muscle (DRM) was isolated from the whole body extract of the starfish, Asterina pectinifera. The peptide was purified by gel-filtration ion-exchange and <TEX>$C_{18}$</TEX> reversed-phase HPLC. The complete amino acid sequence of this peptide, which was determined by automated Edman degradation and MALDI-TOF mass, was Phe-Gly-Lys-Gly-Gly-Ala-Tyr-Asp-Pro-Leu-Ser-Ala-Gly-Phe-Thr-Asp. A comparison of the amino acid sequence with those of other known neuropeptides revealed that the asteripectin was a novel neuropeptide with smooth muscle-relaxing activity on the starfish DRM. This peptide showed threshold response to relaxing activity on the DRM at <TEX>$10^{-10}M$</TEX> and the maximal relaxing effect was <TEX>$120{\pn}7.0\%$</TEX> at <TEX>$10^{-5}M$</TEX>. The relaxing activity of this peptide on the starfish DRM increased in a dose-dependent manner.
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