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Purification and sequence determination of heat‐stable enterotoxin elaborated by a cholera toxin‐producing strain of Vibrio cholerae O1
Author(s) -
Yoshino Ken-ichi,
Miyachi Miki,
Takao Toshifumi,
Bag Prasanta K.,
Xiaozhe Huang,
Nair G.Balakrish,
Takeda Tae,
Shimonishi Yasutsugu
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81766-s
Subject(s) - vibrio cholerae , cholera toxin , enterotoxin , vibrionaceae , toxin , peptide sequence , strain (injury) , amino acid , heat stable enterotoxin , vibrio , chemistry , biochemistry , disulfide bond , biology , microbiology and biotechnology , bacteria , escherichia coli , gene , genetics , anatomy
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.