GANGLIOSIDE GD3 ENHANCES ADHERENCE OF BOTULINUM AND TETANUS NEUROTOXINS TO BOVINE BRAIN SYNAPSIN-I

Tetanus toxin (TTx) and botulinum toxin serotype A (BTxA), preincubate d with trisialoganglioside GT1b, adhere to proteins present on blots o f bovine synaptosomal proteins. Differential solubilization and ammoni um sulfate fractionation provided material enriched in two proteins th at appeared to be adhered to most strongly by the labeled neurotoxins. After excision of the appropriate bands from blots of electrophoretic ally separated proteins, N-terminal amino acid sequence analysis permi tted identification of the proteins as synapsins Ia and lb. Comparison of the effectiveness of different gangliosides at enhancing adherence of the neurotoxins to blots of synapsins la and lb indicated that GD3 was most effective.