产肠毒素大肠杆菌产生的热稳定肠毒素具有完全肠毒素活性的必需结构。
Essential structure for full enterotoxigenic activity of heat-stable enterotoxin produced by enterotoxigenic Escherichia coli.
作者信息
Yoshimura S, Ikemura H, Watanabe H, Aimoto S, Shimonishi Y, Hara S, Takeda T, Miwatani T, Takeda Y
出版信息
FEBS Lett. 1985 Feb 11;181(1):138-42. doi: 10.1016/0014-5793(85)81129-7.
Several analogues of heat-stable enterotoxins (STh and STp) produced by enterotoxigenic Escherichia coli were synthesized. Peptides (STh[6-18] and STp[5-17]) consisting of 13 amino acid residues from the Cys residue near the N-terminus to the Cys residue near the C-terminus and linked by three disulfide bonds had the same biological and immunological properties as native STh and STp, respectively. The results indicated that the sequence with the 13 amino acid residues and three disulfide linkages is essential for full biological activity of ST.
合成了产肠毒素大肠杆菌产生的几种热稳定肠毒素（STh和STp）类似物。由从靠近N端的半胱氨酸残基到靠近C端的半胱氨酸残基的13个氨基酸残基组成、通过三个二硫键连接的肽（STh[6 - 18]和STp[5 - 17]）分别具有与天然STh和STp相同的生物学和免疫学特性。结果表明，具有13个氨基酸残基和三个二硫键连接的序列对于ST的完全生物学活性至关重要。
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