Abstract
The glycine receptor is a ligand-gated anion channel protein of postsynaptic membranes. We expressed a homo-oligomeric receptor composed of human α1 subunits in Spodoptera frugiperda cells by infection with a recombinant Autographa californica nuclear polyhedrosis virus. A substantial fraction of the recombinant receptor was incorporated as a functional channel protein into the cell's plasma membrane at expression levels 4-to 30-fold higher than in other eukaryotic heterologous expression systems or native rat spinal cord membranes, respectively. Upon detergent solubilization, the al receptor was found to exist in a predominantly monodisperse state and could be affinity-purified to near homogeneity. This preparation is a potential starting point for future crystallisation studies.
Original language | English |
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Pages (from-to) | 495-499 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 368 |
Issue number | 3 |
DOIs | |
State | Published - 24 Jul 1995 |
Externally published | Yes |
Keywords
- Affinity purification
- Baculovirus
- Glycine receptor
- Heterologous expression