• 한국수산과학회지
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• 제45권4호
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• pp.358-366
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• 2012

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.

• 한국수산과학회지
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• 제36권1호
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• pp.30-34
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• 2003

Hagfish bradykinin (BK)-related peptide가 먹장어 (E. burgeri)의 피부추출물로부터 분리, 정제되어졌다. 분자량이 875.8 Da인 hagfish BK는 $C_{18}$ 역상 및 양이온교환 high performance liquid chromatography로 순수하게 정제되었다. 자동아미노산서열분석기와 MALDI-TOF mass spectroscopy에서 얻은 결과의 조합으로 hagfish BK의 일차구조는 Gly-Thr-Ala-Gly-Ile-Gly-Pro-Phe-Arg로 판명되었다. 이 아미노산서열을 mammalian BK와 비교하면 다섯 개의 아미노산의 치환을 $(Arg^1{\rightarrow}Gly,\;Pro^2{\rightarrow}Thr,\;Pro^3{\rightarrow}Ala,\;Phe^5{\rightarrow}Ile,\;Ser^6{\rightarrow}Gly)$ 포함한다. Hagfish BK는 먹장어 장관에 대해 수축활성을 나타냈으며, 약 $10^{-11}\;M$의 농도에서 역치반응이 나타났다.