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 $(Arg^1{ ightarrow}Gly,;Pro^2{ ightarrow}Thr,;Pro^3{ ightarrow}Ala,;Phe^5{ ightarrow}Ile,;Ser^6{ ightarrow}Gly)$ 포함한다. Hagfish BK는 먹장어 장관에 대해 수축활성을 나타냈으며, 약 $10^{-11};M$의 농도에서 역치반응이 나타났다.
A hagfish bradykinin(BK)-related peptide was isolated and characterized from the skin of hagfish, Eptatretus burgeri. The hagfish BK with a molecular mass of 875.8 Da was purified to a homogeneity using $C_{18}$ reverse-phase and cation-exchange high performance liquid chromatography. The primary structure of the hagfish BK was determined as Gly-Thr-Ala-Gly-Ile-Gly-Pro-Phe-Arg by a combination of an automated amino acid sequencing and MALDI-TOF mass spectrometry. This amino acid sequence contains five substitutions $(Arg^1{ ightarrow}Gly,;Pro^2{ ightarrow}Thr,;Pro^3{ ightarrow}Ala,;Phe^5{ ightarrow}Ile,;Ser^6{ ightarrow}Gly)$ compared with that of mammalian BK. The hagfish BK showed a contractile action on the intestine of hagfish, Eptatretus burgeri. The threshold concentration of hagfish BK was around $10^{-11};M.$
