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- W2043843023 abstract "The high affinity binding of the neurotransmitter acetylcholine (AcCh) to the nicotinic acetylcholine receptor (nAcChR) of the electric organ of Torpedo californica exhibits a pronounced hysteresis and scanning loops. Dialysis conditions lead to an equilibrium binding curve which is coincident with the upper hysteresis branch; K = 5 × 10−9M, 4° C; and one AcCh molecule binds to the receptor (R) monomer of Mr ≈ 290 000. Kinetic analysis of the changes in free and bound AcCh during the open-system conditions of dialysis, which releases the metastability, shows that AcCh (A) binding proceeds along an induced-fit pathway according to A + Rh ⇌ ARh ⇌ ARvh, describing the ligand-induced transition from the high affinity state (Rh; Kh ≈ 10−7M) to the very high affinity state (Rvh; Kvh ⪡ k). The rate constant of the step ARh → ARvh is k2 = 6 × 10−3 s−1 and that of the reverse s is k−2 = 3 × 10−4 s−1. Direct binding of A to free Rvh can be neglected. Therefore, the state Rvhdoes not pre-exist; it is induced and only stable, as ARvh, by bound AcCh. The metastability can be described in terms of long-lived ARvh·R1 hybrid dimers. Physiologically, the steric hindrance in the metastable hybrid may be viewed as a saving device: the functionally important, receptor channel-active R1 conformer is, at low AcCh concentrations ([A] < 1 μM), prevented from converting into the desensitized states Rh and ARvh." @default.
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- W2043843023 date "1988-12-01" @default.
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- W2043843023 title "Scanning curves and kinetics of the acetylcholine/acetylcholine receptor hysteresis" @default.
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- W2043843023 doi "https://doi.org/10.1016/s0302-4598(98)80004-4" @default.
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