Abstract:
:Antibodies were made to a thirteen amino acid synthetic peptide corresponding to the C-terminal portion of the glutamate (glu) receptor, GluR-A. The immunoprecipitation of kainic acid (KA) and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) binding sites by the anti-peptide antibodies was studied using a detergent-solubilized preparation of rat brain membranes. Under these conditions a subpopulation of AMPA binding sites was recognized by the antibodies, but no KA binding sites were recognized. Scatchard analysis of this subpopulation of AMPA binding sites yields a curvilinear plot which fits a two-site model with dissociation constants of 4.6 and 323 nM. These studies show that the glu receptor complex, GluR-A, binds AMPA but not KA and suggest that (i) the binding sites for these two ligands reside on different proteins, and (ii) the KA receptor identified physiologically is not equivalent to the KA binding sites identified with 3H-labelled KA.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wenthold RJ,Hunter C,Wada K,Dechesne CJdoi
10.1016/0014-5793(90)80529-rsubject
Has Abstractpub_date
1990-12-10 00:00:00pages
147-50issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)80529-Rjournal_volume
276pub_type
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