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XB-ART-22384
FEBS Lett 1993 Jul 26;3272:241-6.
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Homomeric and native alpha 7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex.

Anand R , Peng X , Lindstrom J .


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Sucrose gradient analysis of chick acetylcholine receptor (AChR) alpha 7 subunits expressed in oocytes indicates that they form pharmacologically active homomers of the same size as native alpha 7 AChRs, a size compatible with a complex of five alpha 7 subunits. By immunoisolating the [35S]methionine-labeled alpha 7 subunits we also demonstrate that they do not appear to assemble with endogenous Xenopus AChR subunits. Pharmacological characterization of detergent-solubilized brain alpha 7 AChRs and alpha 7 homomers reveals that they have similar but nonidentical properties. The pharmacological difference is most accentuated for cytisine (approximately 50-fold). Thus, at least in E18 chicken brain, most or all of the native alpha 7 AChRs do not appear to be homomeric.

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