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Characterisation of Na + ‐Independent L‐[ 3 H]Glutamate Binding Sites in Human Temporal Cortex
Author(s) -
Cowburn R. F.,
Hardy J. A.,
Roberts P. J.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb02491.x
Subject(s) - kainate receptor , glutamate receptor , amino acid , binding site , population , biology , stereochemistry , chemistry , ampa receptor , biochemistry , receptor , medicine , environmental health
The binding of L‐[ 3 H]glutamate to membranes from human temporal cortex was studied in the absence of Na + , Ca 2+ , and Cl − ions. Pharmacological characterisation revealed that approximately 35% of specific binding at 50 n M L‐[ 3 H]glutamate was sensitive to a combination of kainate and α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionic acid. The remaining approximately 65% of specific binding was to a single population of sites with a K D of 844 n M and a B max of 0.92 pmol/mg protein. The pharmacological characteristics were consistent with an interaction at the N ‐methyl‐D‐aspartate subclass of excitatory amino acid receptor. The inclusion of Cl − ions revealed additional glutamate binding; this was sensitive to quisqualate and DL‐2‐amino‐4‐phosphonobutyrate, but not to kainate, DL‐2‐amino‐7‐phosphonoheptanoate, or α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionic acid.