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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Purification and characterization of a novel neuropeptide from the skin of snakehead fish (Ophicephalus argus)

등록일
2008년 8월 12일 11시 26분 31초
접수번호
1228
발표코드
33P227포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
고혜진, 박남규
부경대학교 생물공학과, Korea
A novel neuropeptide was isolated from the skin of snakehead fish by using the dorsal retractor muscle (DRM) of starfish (Asterina pectinifera) as the bioassay system. The sequence of the purified peptide was analyzed by an automated amino acid sequencing and MALDI-TOF mass spectrophotometry. Molecular ion peak in the MALDI-TOF mass spectrum of the peptide was displayed m/z 484.70 (M+H)+. The primary structure of the purified peptide was determinated as P-A-L-A-L. To investigate the complete primary structure of PALAL, PALAL-OH and PALAL-NH2 were synthesized, and chemical and pharmacological properties of the synthetic peptides were compared with those of native peptide. Both native peptide and the synthetic PALAL-OH indicated identical behaviors on the reverse-phase and cation-exchange HPLC chromatogram, in which the primary structure of native peptide turned out to be PALAL-OH. Synthetic PALAL-OH showed contractile activity at a threshold concentration of approximately 10-8 M and the maximal contractile effect (Emax) was 294±45.4 % at 10-5M on the starfish DRM. However, PALAL-NH2 was inactive even at higher concentration, 10-5M

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