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Characterisation of Na+-independent L-[3H]glutamate binding sites in human temporal cortex.

Cowburn, RF; Hardy, JA; Roberts, PJ; (1988) Characterisation of Na+-independent L-[3H]glutamate binding sites in human temporal cortex. J Neurochem , 50 (6) pp. 1872-1878.

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Abstract

The binding of L-[3H]glutamate to membranes from human temporal cortex was studied in the absence of Na+, Ca2+, and Cl- ions. Pharmacological characterisation revealed that approximately 35% of specific binding at 50 nM L-[3H]glutamate was sensitive to a combination of kainate and alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid. The remaining approximately 65% of specific binding was to a single population of sites with a KD of 844 nM and a Bmax 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 alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid.

Type: Article
Title: Characterisation of Na+-independent L-[3H]glutamate binding sites in human temporal cortex.
Location: England
Keywords: 2-Amino-5-phosphonovalerate, Aged, Amino Acids, Aminobutyrates, Cell Membrane, Chlorides, Glutamates, Glutamic Acid, Humans, Ibotenic Acid, Kainic Acid, Male, Middle Aged, Oxadiazoles, Quisqualic Acid, Receptors, N-Methyl-D-Aspartate, Receptors, Neurotransmitter, Sodium, Temporal Lobe, alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Neurology
UCL > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Neurology > Molecular Neuroscience
URI: http://discovery.ucl.ac.uk/id/eprint/1358902
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