Baculovirus-driven expression and purification of glycine receptor α1 homo-oligomers

Joachim Morr, Nils Rundström, Heinrich Betz, Dieter Langosch, Bertram Schmitt

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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 languageEnglish
Pages (from-to)495-499
Number of pages5
JournalFEBS Letters
Issue number3
StatePublished - 24 Jul 1995
Externally publishedYes


  • Affinity purification
  • Baculovirus
  • Glycine receptor
  • Heterologous expression


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