Abstract
We have purified a nicotinic acetylcholine receptor from rat brain by use of an acetylcholine affinity resin commonly employed for the purification of nicotinic acetylcholine receptor from electric tissue. Receptor, specifically eluted with nicotine, bound (-)-[ 3H]nicotine with a dissociation constant of ∼21 nM. Binding was inhibited by carbamylcholine but not by α-bungarotoxin. Polyacrylamide gel electrophoresis yielded two protein bands, of apparent mol.wts. 80,400 and 52,400. These results provide independent confirmation of the subunit size and composition reported for rat brain nicotinic receptor isolated by immunoaffinity methods and demonstrate a method of purification that can be performed with commercially available reagents.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
