The effects of temperature, pH and sodium dodecyl sulfate on the conformation of the enterotoxin from Clostridium perfringens type A were followed by circular dichroism in both the peptide and aromatic regions. At near-physiological conditions (35 degrees C, pH 6.7) the enterotoxin exhibited a conformation consisting of approximately 60% pleated sheet, 40% non-periodic, and essentially no helix. The peptide region was relatively stable at temperatures up to 55 degrees C and at pH values ranging from 4-10. The aromatic region demonstrated profound, time-dependent changes at 55 degrees C. At temperatures greater than 55 degrees C, extremes of pH, and in the presence of SDS, the spectra in both regions showed major structural reorganization; in most cases a gain in helical content at the expense of sheet structure was observed. The conformational properties of the protein are very similar to those observed for the lectins, a group of carbohydrate-binding proteins.
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