FEBS Letters | |
Purification and sequence determination of heat‐stable enterotoxin elaborated by a cholera toxin‐producing strain of Vibrio cholerae O1 | |
Miyachi, Miki2  Takeda, Tae1  Xiaozhe, Huang1  Nair, G.Balakrish3  Yoshino, Ken-ichi2  Shimonishi, Yasutsugu2  Takao, Toshifumi2  Bag, Prasanta K.3  | |
[1] Department of Infectious Diseases Research, National Children's Medical Research Center, Taishido 3-35-31, Setagaya-ku, Tokyo 154, Japan;Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565, Japan;National Institute of Cholera and Enteric Diseases, P-33, CIT Scheme XM, Beliaghata, Calcutta-700 010, India | |
关键词: Heat-stable enterotoxin; Primary structure; Cholera; Vibrio cholerae O1; | |
DOI : 10.1016/0014-5793(93)81766-S | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Four molecular species of heat-stable enterotoxins elaborated by a cholera toxin-producing strain of Vibrio cholerae O1 were isolated from its culture supernatant. The amino acid sequence of one of the enterotoxins was determined to be Phe-Ile-Lys-Gln-Val-Asp-Glu-Asn-Gly-Asn-Leu-Ile-Asp-Cys-Cys-Glu-Ile-Cys-Cys-Asn-Pro-Ala-Cys-Phe-Gly-Cys-Leu-Asn with three intramolecular disulfide linkages. The other enterotoxins had shorter amino acid sequences in the N-terminal regions, but possessed the same sequence in their C-terminal regions including the three disulfide linkages. The enterotoxins with the shorter N-terminal sequences showed more potent toxicities, and the minimum effective dose of the longest one with 28 amino acid residues was 10-folds of that of the shortest one.
【 授权许可】
Unknown
【 预 览 】
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