TY - JOUR
T1 - Biological activity of synthetic peptides analogous to heat-stable enterotoxin produced by Yersinia enterocolitica
AU - Inoue, Takashi
AU - Yukitake, Jun
AU - Hara, Susumu
AU - Okamoto, Keinosuke
AU - Miyama, Akio
N1 - Funding Information:
This work was supported by a Grant-in-Aid for Special Project research, The Ministry of Education, Science and Culture and a Grant (59-294) from The Ishida Foundation.
PY - 1986/9
Y1 - 1986/9
N2 - 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.
AB - 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.
KW - Yersinia enterocolitica
KW - heat-stable enterotoxin
KW - synthetic peptide analogues
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U2 - 10.1111/j.1574-6968.1986.tb01685.x
DO - 10.1111/j.1574-6968.1986.tb01685.x
M3 - Article
AN - SCOPUS:0022539507
SN - 0378-1097
VL - 36
SP - 151
EP - 153
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
IS - 2-3
ER -