Mode of disulfide bond formation of a heat‐stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli

FEBS Letters

Takeda, Tae³  Hane, Motomu¹  Aimoto, Saburo¹  Koizumi, Michiyuki¹  Shimonishi, Yasutsugu¹  Hidaka, Yuji¹  Takeda, Yoshifumi⁴  Miwatani, Toshio² 

[1] Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan;Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan;National Children's Medical Research Center, Setagaya-ku, Tokyo 154, Japan;The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108, Japan

关键词: Thermal stability;    Enterotoxin;    Disulfide bond;    (E. coli);   

DOI  :  10.1016/0014-5793(87)80134-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To determine the modes of three disulfide linkages in the heat-stable enterotoxin (ST_h) produced by a human strain of enterotoxigenic Escherichia coli, we synthesized ST_h(6–18), which consists of 13 amino acid residues and has the same intramolecular disulfide linkages as native ST_h [(1985) FEBS Lett. 181, 138–142], by stepwise and selective formation of disulfide bonds using different types of removable protecting groups for the Cys residues. Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard ST_h(6–18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in ST_h(6–18) are

【 授权许可】

Unknown