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pubmed-article:2060767pubmed:abstractTextTo characterize an acceptor for Clostridium botulinum type B neurotoxin, its binding kinetics were examined with mouse brain synaptosomes treated with various enzymes. The amount of 125I-labelled neurotoxin bound to synaptosomes decreased upon treatment with lysyl endopeptidase, neuraminidase, or phospholipase C. The binding of the neurotoxin was partially recovered by incubation of neuraminidase-treated synaptosomes with ganglioside GT1b or GD1a. Gangliosides incorporated into untreated, lysyl endopeptidase-treated, and phospholipase C-treated synaptosomes had no effect on the binding of the neurotoxin. These results may suggest that type B neurotoxin binds to gangliosides in cooperation with a certain protease-sensitive substance on the neural membranes.lld:pubmed
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pubmed-article:2060767pubmed:articleTitleProperties of a protease-sensitive acceptor component in mouse brain synaptosomes for Clostridium botulinum type B neurotoxin.lld:pubmed
pubmed-article:2060767pubmed:affiliationDepartment of Veterinary Science, College of Agriculture, University of Osaka Prefecture, Japan.lld:pubmed
pubmed-article:2060767pubmed:publicationTypeJournal Articlelld:pubmed