Purification and characterization of Escherichia coli heat-stable enterotoxin II

Y. Fujii, M. Hayashi, S. Hitotsubashi, Y. Fuke, H. Yamanaka, K. Okamoto

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


Escherichia coli heat-stable enterotoxin II (STII) was purified to homogeneity by successive column chromatographies from the culture supernatant of a strain harboring the plasmid encoding the STII gene. The purified STII evoked a secretory response in the suckling mouse assay and ligated rat intestinal loop assay in the presence of protease inhibitor, but the response was not observed in the absence of the inhibitor. Analyses of the peptide by the Edman degradation method and fast atom bombardment mass spectrometry revealed that purified STII is composed of 48 amino acid residues and that its amino acid sequence was identical to the 48 carboxy-terminal amino acids of STII predicted from the DNA sequence (C. H. Lee, S. L. Moseley, H. W. Moon, S.C. Whipp, C. L. Gyles, and M. So, Infect. Immun. 42:264-268, 1983). STII has four cysteine residues which form two intramolecular disulfide bonds. Two disulfide bonds were determined to be formed between Cys-10-Cys-48 and Cys-36 by analyzing tryptic hydrolysates of STII.

Original languageEnglish
Pages (from-to)5516-5522
Number of pages7
JournalJournal of bacteriology
Issue number17
Publication statusPublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


Dive into the research topics of 'Purification and characterization of Escherichia coli heat-stable enterotoxin II'. Together they form a unique fingerprint.

Cite this