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By Solomon Kadis (Auth.)

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Extra resources for Bacterial Protein Toxins

Sample text

By Andrews' method (1965) the molecular weights of the three subfractions of /3, desig­ nated as j8 l5 /3 2, and j83 (Fig. 7), appeared to be 290,000, 500,000, and 900,000, respectively. 15 M Tris-HCl buffer, pH 8, dissociated each of the components into four peaks, the first eluting in the position of a and the others in the same positions of Z^, /3 2, and /33. , 1966). From these molecular weights and from their common biological activity, these hemagglutinin components appeared to be one entity in different states of aggregation.

Than that of the starting material (Table IX). They also measured the dif­ fusion rate of the crystalline toxin in agar gel and found that they could separate toxin from hemagglutinating agents and that toxin migrated much faster than did hemagglutinin. Based on the diffusion rate, the mo­ lecular weight of the toxin was estimated to be between 10,000 and 20,000 (Schantz and Lauffer, 1962). We have already mentioned that Wagman (1963) observed a dialyzable toxin with an estimated molecular weight of 3800 by treating the crystalline toxin with alkali at pH 9 and then hydrolyzing it with pepsin.

The authors concluded that except for small differences there was a remarkable simi­ larity in the overall ratios among the individual amino acids. What was completely overlooked was that the concentrations of at least seven of the corresponding amino acids in their toxin and the crystalline toxin were significantly different. In addition, if the low molecular weight toxin was pure, it should not have been compared with crystalline toxin which had b>c - - Reprinted by permission from V a n A l s t y n e et al (1966).

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