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Primary structure of heat-stable enterotoxin produced by Yersinia enterocolitica
Biochemical and Biophysical Research Communications
|December 28, 1984
Abstract:
A heat-stable enterotoxin was isolated and purified from the culture supernatant of Yersinia enterocolitica by reversed-phase high-performance liquid chromatography. The amino acid sequence of the purified toxin was determined to be as follows: (sequence; see text) (X: not determined). The C-terminal sequence containing 6 half-cystine residues was highly homologous to that of heat-stable enterotoxin of enterotoxigenic Escherichia coli.