Primary structure determination of Escherichia coli heat-stable enterotoxin of porcine origin

Abstract

The chemical characterization of Escherichia coli heat-stable enterotoxin (ST) is described. The toxin was isolated and purified to homogeneity from the E. coli strain F11 (PI55) of porcine origin. Following quantitative amino acid analysis, the enterotoxin was found to contain 18 amino acids including 6 cysteines, but was devoid of Ser, Val, Met, Ile, Lys, His, and Arg residues. All cysteine residues were found to be involved in disulfide bridges, even though their positions could not be localized. The enterotoxin thus has a molecular weight of 1979 and was shown to be an octadecapeptide with the following sequence: H2N-Asn-Thr-Phe-Tyr-Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Ala-Gly-Cys-Tyr-COOH. Its relationship to other known enterotoxins is discussed.