• 한국수산과학회지
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• 제45권2호
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• pp.114-121
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• 2012

A novel neuropeptide was isolated from the skin of the snakehead Channa argus using the dorsal retractor muscle (DRM) of a starfish Asterina pectinifera as a bioassay system. The amino acid sequence of the purified peptide was analyzed using automated sequencing and MALDI-TOF mass spectrophotometry. The primary structure of the purified peptide was determined to be Pro-Ala-Leu-Ala-Leu. To investigate the complete primary structure of this peptide, Pro- Ala-Leu-Ala-Leu-OH and Pro-Ala-Leu-Ala-Leu-NH2 were synthesized. The chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. Both the native peptide and synthetic Pro-Ala- Leu-Ala-Leu-OH had identical behaviors on the reverse-phase and cation-exchange HPLC chromatograms. Synthetic Pro-Ala-Leu-Ala-Leu-OH showed contractile activity on the DRM, and the threshold concentration of this peptide was approximately $10^{-8}$ M. The maximal contractile effect ($E_{max}$) of this peptide was $294{\pm}45.4$% at $10^{-5}$ M.

• 한국수산과학회지
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• 제38권3호
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• pp.148-152
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• 2005

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 $C_{18}$ 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 $10^{-10}M$ and the maximal relaxing effect was $120{\pn}7.0\%$ at $10^{-5}M$. The relaxing activity of this peptide on the starfish DRM increased in a dose-dependent manner.

• 한국수산과학회지
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• 제47권2호
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• pp.129-134
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• 2014

Two neuropeptides were purified from the acidified tube feet extract of the starfish Asterias amurensis by C18 reversed phase and size-exclusion high-performance liquid chromatography (HPLC). The tube feet extract and the purified peptides (AST-I and AST-II) showed potent contractile activity on dorsal retractor muscle (DRM) of the starfish Asterina pectinifera and intestine (smooth muscle) of the panther puffer Takifugu pardalis. Treatment of the purified peptides with dithiothreitol (DTT) for 60 min at $37^{\circ}C$ significantly altered their retention times, suggesting that these compounds contained disulfide bonds. The molecular weights of AST-I and AST-II were determined to be 2064.2 Da and 6137.2 Da, respectively, by MALDI-TOF mass spectrometry.

• 생명과학회지
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• 제24권5호
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• pp.491-497
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• 2014

아무르불가사리(Asterias amurensis)의 6가지의 조직 추출물들을 사용하여 항균활성, 항산화 활성 및 평활근에 대한 수축과 이완반응에 대한 활성을 측정하였다. 1% (v/v) 초산용액을 사용하여 동결 건조한 샘플들을 추출하여 각각의 활성측정에 사용한 결과, 껍질을 제외한 모든 조직 추출물들은 E. coli D31에 대해 강한 항균활성을 나타내었고, 근육 및 장관 추출물들은 별불가사리(Asterina pectinifera)의 DRM에 대해 수축반응을 나타냈다. 한편, 오징어(Todarodes pacificus) 식도에 대한 수축반응은 실험에 사용한 모든 조직 추출물들에서 검출되었다. 특히, 간 추출물의 수축활성은 다른 조직의 추출물의 활성에 비해 더 높았다. 뿐만 아니라 간, 근육 및 소화관 추출물은 졸복(Takifugu pardalis)의 장관에 대해서 수축반응을 나타냈다. 별불가사리의 DRM에 대한 이완반응은 실험에 사용한 모든 조직 추출물들에서 활성을 나타냈다. 항산화 활성은 장관, 간 및 껍질의 추출물들에서 강하게 나타났다. 따라서 아무르불가사리는 새로운 생체기능 조절물질의 발견에 대한 가능성을 지닌 자원이라는 것을 본 연구의 결과들은 제시한다.