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

Summary

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.

Yersinia enterocolitica, synthetic peptide analogues, heat-stable enterotoxin