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가물치(Channa argus)로부터 평활근 수축활성 펩타이드의 정제

Isolation of a Novel Neuropeptide with Contractile Activity on the Smooth Muscle from the Snakehead Channa argus

  • Go, Hye-Jin (Department of Biotechnology, Pukyong National University) ;
  • Park, Nam-Gyu (Department of Biotechnology, Pukyong National University)
  • 투고 : 2012.02.08
  • 심사 : 2012.04.16
  • 발행 : 2012.04.30

초록

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.

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참고문헌

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