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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
1989-9-12
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pubmed:abstractText |
The membrane bound acetylcholine receptor from Torpedo marmorata was photolabeled by the noncompetitive channel blocker ]3H]chlorpromazine under equilibrium conditions in the presence of the agonist carbamoylcholine. The radioactivity incorporated into the AChR subunits was reduced by addition of phencyclidine, a specific ligand for the high-affinity side for noncompetitive blockers. The alpha-subunit was purified and digested with trypsin and/or CNBr and the resulting fragments fractionated by HPLC. Sequence analysis resulted in the identification of Ser-248 as a major residue labeled by [3H]chlorpromazine in a phencyclidine-sensitive manner. This residue is located in the hydrophobic and putative transmembrane segment M2 of the alpha-subunit, a region homologous to that containing the chlorpromazine-labeled Ser-262 in the delta-chain [1] and Ser-254 and Leu-257 in the beta-chain [2]. Extended sequence analysis of the hydrophobic segment M1 further showed that no labeling-occurred in this region.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
190-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2474458-Amino Acid Sequence,
pubmed-meshheading:2474458-Animals,
pubmed-meshheading:2474458-Binding Sites,
pubmed-meshheading:2474458-Chlorpromazine,
pubmed-meshheading:2474458-Cyanogen Bromide,
pubmed-meshheading:2474458-Ion Channels,
pubmed-meshheading:2474458-Molecular Sequence Data,
pubmed-meshheading:2474458-Peptide Mapping,
pubmed-meshheading:2474458-Receptors, Nicotinic,
pubmed-meshheading:2474458-Torpedo
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pubmed:year |
1989
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pubmed:articleTitle |
The noncompetitive blocker [(3)H]chlorpromazine labels segment M2 but not segment M1 of the nicotinic acetylcholine receptor alpha-subunit.
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pubmed:affiliation |
URA CNRS 0210, Départment des Biotechnologies, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article,
In Vitro
|