Summary
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1.
Labeling of crystalline botulinum A toxin has been done with 125I by aid of the chloramine T method. The neurotoxic component is well preserved, whereas the hemagglutinin undergoes physicochemical alterations. Neither with labeled nor with unlabeled toxin, hemagglutinating power parallels the main protein peak.
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2.
Neurotoxin, homogeneous in gel filtration, is bound to synaptosomes from rat brain. Cold toxin competes with labeled toxin, and antitoxin or neuraminidase partially remove the bound neurotoxin.
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3.
Upon intramuscular injection, some radioactivity is recovered in the respective parts of the spinal cord. Antitoxin prevents the ascent.
The similarities between tetanus and botulinum A neurotoxins are stressed.
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References
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Habermann, E. 125I-labeled neurotoxin from clostridium botulinum A: Preparation, binding to synaptosomes and ascent to the spinal cord. Naunyn-Schmiedeberg's Arch. Pharmacol. 281, 47–56 (1974). https://doi.org/10.1007/BF00500611
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DOI: https://doi.org/10.1007/BF00500611