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- W59491181 abstract "[3H]Kainic acid ([3H]KA) is a widely used tool for studying the KA class of excitatory amino acid receptors. [3H]KA of significantly higher specific activity has become available permitting use of radioligand concentrations below the dissociation constant (K(D)) of the high-affinity binding site. We employed low radioligand (0.05-0.2 nM) and receptor concentrations (0.01 nM) to gain new insights into the binding characteristics of the high-affinity KA binding site in a standard preparation of lyzed synaptosomal membranes from the cerebral cortex of male Sprague-Dawley rats. Under these conditions, KA binds to a single class of high-affinity sites with a K(D) of 1.0+/- 0.3 nM. The potencies of competing agents are considerably higher than published reports. Specifically, domoic acid, glutamate, and glutamine exhibit IC(50) values for displacing [3H]KA of 0.37+/-0.02, 94+/-13, and 1500+/-500 nM, respectively. Domoate (1 microM) was tested against a panel of 32 central nervous system binding sites and found to be inactive at each, indicating this toxin displays considerable selectivity. This study illustrates the remarkable potency of domoic acid and underlines the importance of performing radioligand binding studies at concentrations of constituents that permit characterization of high-affinity interactions." @default.
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- W59491181 date "1999-11-01" @default.
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- W59491181 title "High-affinity [3H] kainic acid binding to brain membranes" @default.
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- W59491181 doi "https://doi.org/10.1016/s1056-8719(00)00040-x" @default.
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