Abstract
Summary
Botulinal toxins (types A, E and F), in forms of two chain proteins of MW 150,000, lost more than 99% of their toxicity when incubated with the disulfide reducing agent dithiothreitol. Type E progenitor toxin, which is a single chain protein of MW 150,000, showed a comparable loss of toxicity during similar treatment. Results indicate the importance of disulfide bonds in holding these proteins in the configuration that is critical for their biological activity.
The authors thank Mrs. Kaoruko Mizutani for her excellent technical assistance and Dr. E. J. Schantz for the crystalline type A toxin. Research was supported by the College of Agricultural and Life Sciences, University of Wisconsin, Madison, by Grant FD-09000 of the U.S. Public Health Service and contributions from various food companies.
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