Abstract
The acceptor for Clostridium botulinum type B neurotoxin was solubilized from rat brain synaptic membrane with nonionic detergent, nonanoyl-N-methylglucamide (MEGA-9). The solubilized acceptor was assayed for the binding activity by precipitating the acceptor with acetone in the presence of phosphatidylcholine. 125Ilabeled neutroxin specifically bound to the lipid vesicles having incorporated the acceptor together with gangliosided. The lipid vesicles having incorporated either the acceptor or gangliosides alone showed extremely low binding activity. The treatment of the solubilized acceptor with lysyl endopeptidase and accompanying an N-linked carbohydrate moiety. The observations suggest also that a protein acceptor/ganglioside complex may be required to form the functional toxin receptor.
| Original language | English |
|---|---|
| Pages (from-to) | 333-338 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta - General Subjects |
| Volume | 1158 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 28 1993 |
| Externally published | Yes |
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Keywords
- (C. botulinum)
- Ganglioside
- Neurotoxin
- Protein acceptor
- Solubilization
- Synaptic membrane
- Toxin binding
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Solubilization and characterization of the acceptor for Clostridium botulinum type B neutroxin from rat brain synaptic membranes. / Nishiki, Tei-ichi; Ogasawara, Jun; Kamata, Yoichi; Kozaki, Shunji.
In: Biochimica et Biophysica Acta - General Subjects, Vol. 1158, No. 3, 28.11.1993, p. 333-338.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solubilization and characterization of the acceptor for Clostridium botulinum type B neutroxin from rat brain synaptic membranes
AU - Nishiki, Tei-ichi
AU - Ogasawara, Jun
AU - Kamata, Yoichi
AU - Kozaki, Shunji
PY - 1993/11/28
Y1 - 1993/11/28
N2 - The acceptor for Clostridium botulinum type B neurotoxin was solubilized from rat brain synaptic membrane with nonionic detergent, nonanoyl-N-methylglucamide (MEGA-9). The solubilized acceptor was assayed for the binding activity by precipitating the acceptor with acetone in the presence of phosphatidylcholine. 125Ilabeled neutroxin specifically bound to the lipid vesicles having incorporated the acceptor together with gangliosided. The lipid vesicles having incorporated either the acceptor or gangliosides alone showed extremely low binding activity. The treatment of the solubilized acceptor with lysyl endopeptidase and accompanying an N-linked carbohydrate moiety. The observations suggest also that a protein acceptor/ganglioside complex may be required to form the functional toxin receptor.
AB - The acceptor for Clostridium botulinum type B neurotoxin was solubilized from rat brain synaptic membrane with nonionic detergent, nonanoyl-N-methylglucamide (MEGA-9). The solubilized acceptor was assayed for the binding activity by precipitating the acceptor with acetone in the presence of phosphatidylcholine. 125Ilabeled neutroxin specifically bound to the lipid vesicles having incorporated the acceptor together with gangliosided. The lipid vesicles having incorporated either the acceptor or gangliosides alone showed extremely low binding activity. The treatment of the solubilized acceptor with lysyl endopeptidase and accompanying an N-linked carbohydrate moiety. The observations suggest also that a protein acceptor/ganglioside complex may be required to form the functional toxin receptor.
KW - (C. botulinum)
KW - Ganglioside
KW - Neurotoxin
KW - Protein acceptor
KW - Solubilization
KW - Synaptic membrane
KW - Toxin binding
UR - http://www.scopus.com/inward/record.url?scp=0027486425&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027486425&partnerID=8YFLogxK
U2 - 10.1016/0304-4165(93)90032-4
DO - 10.1016/0304-4165(93)90032-4
M3 - Article
C2 - 8251534
AN - SCOPUS:0027486425
VL - 1158
SP - 333
EP - 338
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 3
ER -