Biological activity of synthetic peptides analogous to heat-stable enterotoxin produced by Yersinia enterocolitica

Takashi Inoue, Jun Yukitake, Susumu Hara, Keinosuke Okamoto, Akio Miyama

研究成果査読

抄録

3 peptides were synthesized chemically by following the primary structure of heat-stable enterotoxin (ST) produced by Yersinia enterocolitica. A peptide 1-30, having the whole sequence of 30 amino-acid residues, showed a ST activity similar to that of analogue peptide 15-30 composed of the C-terminal 16 amino acid residues. The c-GMP levels of L cells increased through an interaction with peptide 1-30 but not with peptide 15-30, while membranes isolated from broken L cells responded to both. Peptide 1-11, composed of the N-terminal 11 amino-acid residues, showed no biological activity.

本文言語English
ページ(範囲)151-153
ページ数3
ジャーナルFEMS Microbiology Letters
36
2-3
DOI
出版ステータスPublished - 9月 1986
外部発表はい

ASJC Scopus subject areas

  • 微生物学
  • 分子生物学
  • 遺伝学

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