Abstract
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 noncompetitive inhibitors of NMDARs. Magnesium had little effect on the reconstituted channels.
Original language | English (US) |
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Pages (from-to) | 141-148 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 394 |
Issue number | 2 |
DOIs | |
State | Published - Sep 30 1996 |
Keywords
- Glutamate receptor
- Ion channel reconstitution
- NMDA activation
- Planar bilayer membranes
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology