[Study by a rapid mixing method of the interaction between a fluorescent cholinergic agonist and membrane fragments rich in cholinergic receptors from Torpedo marmorata].
The analysis by stopped-flow of the interaction of fluorescent agonist (C5DACho1) with the acetylcholine receptor in its membrane-bound form reveals several kinetic steps: a fast one, in the millisecond range, associated with the binding of C5DACho1 to a high affinity state and a "medium" and "slow" one, the last one representing possibly an isomerisation of the receptor molecule towards the high affinity state.
D000109:Acetylcholine / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D005399:Fishes; D005456:Fluorescent Dyes; D007700:Kinetics; D008566:Membranes / Q000378:metabolism; D010277:Parasympathomimetics / Q000378:metabolism*; D011318:Prilocaine / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000378:metabolism*
D005456:Fluorescent Dyes; D010277:Parasympathomimetics; D011950:Receptors, Cholinergic; D011318:Prilocaine; D000109:Acetylcholine
Etude par une méthode de mélange rapide de l'interaction d'un agoniste cholinergique fluorescent avec des fragments de membrane riches en récepteur cholinergique de Torpedo marmorata