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Purification and Characterization of [Ala2]-Neuromedin N from the Visceral Tissue of the African Lungfish, Protopterus dolloi

  • Kim, Chan-Hee (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Go, Hye-Jin (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Kim, Eun-Jung (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Seo, Jung-Kil (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Hong, Yong-Ki (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Kim, Hyung-Rak (Faculty of Food Science & Biotechnology, Pukyong National University) ;
  • Chung, Joon-Ki (Department of Aquatic Life Medicine, Pukyong National University) ;
  • Muneoka, Yojiro (Faculty of Integrated Arts and Sciences, Hiroshima University) ;
  • Park, Nam-Gyu (Faculty of Food Science & Biotechnology, Pukyong National University)
  • Published : 2006.11.20

Abstract

A new biologically active peptide with structural similarity to neuromedin N (NMN) has been isolated from extracts of visceral tissue of the African lungfish, Protopterus dolloi, using the rectum of the quail as the bioassay system. The primary structure of NMN-related peptide was established as Lys-Ala-Pro-Tyr-Ile-Leu-OH ([$Ala_2$]-NMN) and contained one substitution ($Ala_2\rightarrow$Ile) compared with the porcine NMN. [$Ala_2$]-NMN was found to have an excitatory effect on rectal muscle tissues of quail (Coturnix japonica), newt (Cynops pyrrhogaster) and black bass (Micropterus sulmoides). The threshold concentration of [Ala2]-NMN for contraction of C. japonica muscle was found to be approximately $10^-11$M. [$Ala_2$]-NMN showed contractile activities in the following order: C. japonica > C. pyrrhogaster > M. sulmoides. The identification of [Ala2]-NMN provides evidence that NMN family, hitherto confined to mammals, has a widespread occurrence in lungfish.

Keywords

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