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Ion channel properties of a protein complex with characteristics of a glutamate/ N ‐methyl‐ d ‐aspartate receptor
Author(s) -
Aistrup Gary L.,
Szentirmay Marilyn,
Kumar Keshava N.,
Babcock Kent K.,
Schowen Richard L.,
Michaelis Elias K.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00938-6
Subject(s) - nmda receptor , glutamate receptor , chemistry , glycine , biophysics , ion channel , receptor , ligand gated ion channel , biochemistry , amino acid , biology
The functional reconstitution of glutamate receptor proteins purified from mammalian brain has been difficult to accomplish. However, channels activated by l ‐glutamate (L‐Glu) and N ‐methyl‐ d ‐aspartate (NMDA) were detected in planar lipid bilayer membranes (PLMs) following the reconstitution of a complex of proteins with binding sites for NMDA receptor (NMDAR) ligands. The presence of glycine was necessary for optimal activation. A linear current‐voltage relationship was observed with the reversal potential being zero. Channels activated by L‐Glu had conductances of 23, 47 and 65 pS, and were suppressed partially by competitive and fully by non‐competitive inhibitors of NMDARs. Magnesium had little effect on the reconstituted channels.