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

作者信息

Cowburn R F, Hardy J A, Roberts P J

机构信息

Department of Biochemistry and Molecular Genetics, St. Mary's Hospital Medical School, Paddington, London, England.

出版信息

J Neurochem. 1988 Jun;50(6):1872-8. doi: 10.1111/j.1471-4159.1988.tb02491.x.

DOI:10.1111/j.1471-4159.1988.tb02491.x
PMID:2897429
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.

摘要

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