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http://dx.doi.org/10.5657/KFAS.2012.0358

Purification of Neuropeptide with the Contractile Activity on the Smooth Muscle from the Skin of Conger Eel Conger myriaster  

Go, Hye-Jin (Department of Biotechnology, Pukyong National University)
Park, Nam-Gyu (Department of Biotechnology, Pukyong National University)
Publication Information
Korean Journal of Fisheries and Aquatic Sciences / v.45, no.4, 2012 , pp. 358-366 More about this Journal
Abstract
A novel neuropeptide was isolated from the skin of the conger eel Conger myriaster using hagfish Eptatretus burgeri intestine as a bioassay system. The sequence of the purified peptide was analyzed using automated amino acid sequencing and MALDI-TOF mass spectrophotometry. The molecular ion peak in the MALDI-TOF mass spectrum of the peptide was at m/z 962.89 $(M+H)^+$. The sequence of the peptide was determined to be L-P-M-L-E-T-Q-M, and was tentatively named comyrin. To investigate the complete primary structure of comyrin, comyrin-OH and comyrin-$NH_2$ were synthesized and the chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. However, the elution time of synthetic peptides did not match that of the native peptide on the reverse-phase HPLC chromatogram. In addition, the synthetic peptides did not cause contractile activity in the intestinal smooth muscle of the hagfish. Based on these results, one possible reason for this disagreement may be the presence of a D-amino acid in comyrin.
Keywords
Neuropeptide; Conger eel; Hagfish intestine;
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