Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non‐identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex

摘要

>Sucrose gradient analysis of chick acetylcholine receptor (AChR) α7 subunits expressed in oocytes indicates that they form pharmacologically active homomers of the same size as native α7 AChRs, a size compatible with a complex of five α7 subunits. By immunoisolating the [35S]methionine-labeled α7 subunits we also demonstrate that they do not appear to assemble with endogenous Xenopus AChR subunits. Pharmacological characterization of detergent-solubilized brain α7 AChRs and α7 homomers reveals that they have similar but nonidentical properties. The pharmacological difference is most accentuated for cytisine (~50-fold). Thus, at least in E18 chicken brain, most or all of the native α7 AChRs do not appear to be homomeric.