Partial Characterization of Bovine Synaptosomal Proteins Adhered to By Botulinum and Tetanus Neurotoxins

  • Cara-Lynne Schengrund
  • Bibhuti R. DasGupta
  • Nancy J. Ringler


Binding of botulinum (BTx) and tetanus (TTx) neurotoxins to synaptic termini has been hypothesized to require a protein component(s)1–3 in addition to gangliosides of the Glb series4,5 (nomenclature described by Svennerhoim6). Results that we obtained in studies of inhibition by gangliosides of the binding of BTxA and TTx to ganglioside GT1b-coated plastic wells indicate that Glb gangliosides do not function as high affinity ligands for the neurotoxins. We observed that the concentration of ganglioside GT1b needed to block binding of either BTxA or TTx to GT1bcoated plastic wells was in the µM range.7 In contrast, when the same assay system was used to determine the concentration of ganglioside GM1 needed to block binding of cholera toxin to GM1-coated plastic wells, nM values were obtained.8


Ammonium Sulfate Cholera Toxin Electric Organ Tetanus Toxin High Affinity Ligand 


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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Cara-Lynne Schengrund
    • 1
  • Bibhuti R. DasGupta
    • 2
  • Nancy J. Ringler
    • 1
  1. 1.Department of Biological ChemistryThe M.S. Hershey Medical CenterHersheyUSA
  2. 2.Department of Food Microbiology and Toxicology University of WisconsinMadisonUSA

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