Abstract
The nicotinic acetylcholine receptor was purified by affinity chromatography in the presence of dioleoylphosphatidylcholine (DOPC). A method for replacing the DOPC with other lipids was developed by using detergent solubilization with a large excess of the new lipid by sucrse density gradient centrifugation in detergent-free buffers to separate receptor-lipid complexes from excess lipid and detergent. Homogeneous complexes of defined lipid composition could be easily prepared and the efficiency of substitution was independent of lipid type. However, the functional properties of the resulting lipid complexes depended on the lipid composition. © 1988.
| Original language | English |
|---|---|
| Pages (from-to) | 359-366 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 944 |
| Issue number | 3 |
| Publication status | Published - 20 Oct 1988 |
Keywords
- (T. califonica)
- Acetylcholine receptor
- Lipid-protein interaction
- Reconstitution