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    
Abstract/OtherAbstract:
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.
Authors:
J Ogasawara; Y Kamata; G Sakaguchi; S Kozaki
Related Documents :
1324537 - Binding of brevetoxins and ciguatoxin to the voltage-sensitive sodium channel and confo...
29897 - Sea anemone toxin and scorpion toxin share a common receptor site associated with the a...
3564027 - Interaction of t-2 toxin with bovine carrier erythrocytes: effects on cell lysis, perme...
22871957 - Androgen receptor antagonism by divalent ethisterone conjugates in castrate-resistant p...
2360217 - Development and characterization of monoclonal antibodies to a specific domain of human...
7084117 - Nonfunctioning progesterone receptors in the developed oviducts from estrogen-withdrawn...
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    
Affiliation:
Department of Veterinary Science, College of Agriculture, University of Osaka Prefecture, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Botulinum Toxins / metabolism*
Brain / metabolism*
Cell Membrane / metabolism
Clostridium botulinum / metabolism
Gangliosides / metabolism
Kinetics
Mice
Neuraminidase / metabolism
Neurotoxins / metabolism*
Radioligand Assay
Serine Endopeptidases / metabolism
Synaptosomes / metabolism*
Type C Phospholipases / metabolism
Chemical
Reg. No./Substance:
0/Botulinum Toxins; 0/Gangliosides; 0/Neurotoxins; EC 3.1.4.-/Type C Phospholipases; EC 3.2.1.18/Neuraminidase; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.50/lysyl endopeptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Demonstration of formaldehyde dehydrogenase activity in formaldehyde-resistant Enterobacteriaceae.
Next Document:  Genetics of subdivided populations and its relationships with certain measures of association.