Title : An inhalational anesthetic binding domain in the nicotinic acetylcholine receptor.

Pub. Date : 1996 Apr 2

PMID : 8610122






5 Functional Relationships(s)
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1 To determine inhalational anesthetic binding domains on a ligand-gated ion channel, I used halothane direct photoaffinity labeling of the nicotinic acetylcholine receptor (nAChR) in native Torpedo membranes. Halothane cholinergic receptor nicotinic alpha 4 subunit Homo sapiens
2 To determine inhalational anesthetic binding domains on a ligand-gated ion channel, I used halothane direct photoaffinity labeling of the nicotinic acetylcholine receptor (nAChR) in native Torpedo membranes. Halothane cholinergic receptor nicotinic alpha 4 subunit Homo sapiens
3 [14C]Halothane photoaffinity labeling of both the native Torpedo membranes and the isolated nAChR was saturable, with Kd values within the clinically relevant range. Halothane cholinergic receptor nicotinic alpha 4 subunit Homo sapiens
4 Unlabeled halothane reduced labeling more than did isoflurane, suggesting differences in the binding domains for inhalational anesthetics in the nAChR. Halothane cholinergic receptor nicotinic alpha 4 subunit Homo sapiens
5 These data suggest multiple similar binding domains for halothane in the transmembrane region of the nAChR. Halothane cholinergic receptor nicotinic alpha 4 subunit Homo sapiens