Document Detail

Properties of a protease-sensitive acceptor component in mouse brain synaptosomes for Clostridium botulinum type B neurotoxin.
MedLine Citation:
PMID:  2060767     Owner:  NLM     Status:  MEDLINE    
To 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.
J Ogasawara; Y Kamata; G Sakaguchi; S Kozaki
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  FEMS microbiology letters     Volume:  63     ISSN:  0378-1097     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  1991 Apr 
Date Detail:
Created Date:  1991-08-05     Completed Date:  1991-08-05     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  351-5     Citation Subset:  IM    
Department of Veterinary Science, College of Agriculture, University of Osaka Prefecture, Japan.
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MeSH Terms
Binding Sites
Botulinum Toxins / metabolism*
Brain / metabolism*
Cell Membrane / metabolism
Clostridium botulinum / metabolism
Gangliosides / metabolism
Neuraminidase / metabolism
Neurotoxins / metabolism*
Radioligand Assay
Serine Endopeptidases / metabolism
Synaptosomes / metabolism*
Type C Phospholipases / metabolism
Reg. No./Substance:
0/Botulinum Toxins; 0/Gangliosides; 0/Neurotoxins; EC 3.1.4.-/Type C Phospholipases; EC; EC 3.4.21.-/Serine Endopeptidases; EC endopeptidase

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