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

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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)151-153
Number of pages3
JournalFEMS Microbiology Letters
Volume36
Issue number2-3
DOIs
Publication statusPublished - Sep 1986
Externally publishedYes

Keywords

  • Yersinia enterocolitica
  • heat-stable enterotoxin
  • synthetic peptide analogues

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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