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• W2020911906 abstract "Using a baculovirus expression vector system, the alpha 2 subunit of the mouse alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA)-selective glutamate receptor (GluR) channel was expressed in Spodoptera frugiperda insect cells. Immunoblotting using the antibody made to the synthetic peptide corresponding to the C-terminus of GluR alpha 2 and [35S]methionine/[35S]cysteine metabolic radiolabeling revealed the major 102-kDa and the minor 98-kDa protein bands. Metabolic radiolabeling with tunicamycin suggested that the two bands correspond to glycosylated and unglycosylated forms, respectively. The recombinant GluR alpha 2 proteins expressed in insect cells were also identified by immunofluorescence staining. The results of [3H]AMPA binding assay using whole cells suggested that, in infected Sf21 cells, binding sites of the GluR alpha 2 proteins were possibly located on the extracellular side. Scatchard analysis of AMPA binding showed the following parameters: Kd = 16 nM, Bmax = 1.9 x 10(5) binding sites per cell or 1 pmol/mg protein in the total particulate fraction. The ligand binding characteristics of the receptors expressed in insect cells were examined. From the effect of various agonists on [3H]AMPA binding of the receptors expressed in insect cells, the rank order potency of agonists was quisqualate > AMPA > L-glutamate > kainate. Thus, the baculovirus-insect cell expression system provides high-efficiency expression of the receptor sufficient to permit structural and functional analyses." @default.
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• W2020911906 date "1994-12-01" @default.
• W2020911906 modified "2023-09-24" @default.
• W2020911906 title "Expression and characterization of the α2 subunit of the α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) -selective glutamate receptor channel in a baculovirus system" @default.
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• W2020911906 doi "https://doi.org/10.1016/0006-8993(94)90280-1" @default.
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