By Solomon Kadis (Auth.)
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Extra info for Bacterial Protein Toxins
The rate of inactivation of the toxin by nitrous acid (half of the activity lost within 35 minutes) was considered to be comparable to the rate of deamination of simple amino acids and rapid as compared with the half-life of tyrosine in the substitution reaction. These data, coupled with the evidence from the reaction of the toxin with ketene, indicated to these authors the es sential nature of the amino groups of the toxin. Stefanye et al. (1964) investigated the effects of a series of guanidinium salts on the toxicity of botulinum toxin and the mechanism through which denaturation by these salts occurs.
13, they were able to show by ultracentrifugation that the toxin exists in the form of two polydispersed components. Partial separa tion of the slowly sedimenting component was achieved with the aid of a preparative rotor. This component was judged to be about 20% of the original toxin and was free from hemagglutinins. 7. The toxicity of this component per milligram of nitrogen was at least as great as that of the parent substance. This toxin was tentatively identified as the ultimate toxic unit of botu linum type A toxin (Wagman and Bateman, 1953).
Types B, C, and D were studied, and though only a from types A and B toxin have been separated in the state of purity and homogeneity comparable to a from crystalline toxin, there are strong indications that types C and D, once the proper conditions for chromatography are found, will also yield a similar component. Indeed, procedures for the production of a high specific activity fraction for the toxin of CI. botulinum type C 6 described by Syuto (1965). The starting material with a toxicity 1 X were 10 (mouse IP) MLD per milliliter was obtained by him from culture fil trates of organisms grown in a medium composed of 2 % bactocasein, 1 % 1.
Bacterial Protein Toxins by Solomon Kadis (Auth.)