Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1989-9-12
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
190-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The noncompetitive blocker [(3)H]chlorpromazine labels segment M2 but not segment M1 of the nicotinic acetylcholine receptor alpha-subunit.
pubmed:affiliation
URA CNRS 0210, Départment des Biotechnologies, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, In Vitro