Anomalous interaction of the acetylcholine receptor protein with the nonionic detergent Triton X-114.
Integral membrane proteins that form water-filled channels through membranes often exist as aggregates of similar or identical subunits spanning the membrane. It has been suggested that the insertion into the membrane of the channel-forming domains of the subunits may impart unusual structural features to the membrane-intercalated portions of the protein. To test this proposal, we have investigated the interaction of a multisubunit channel-forming integral membrane protein, the acetylcholine receptor protein, with the nonionic detergent Triton X-114. Whereas non-channel-forming integral membrane proteins that have heretofore been studied form mixed micelles with the detergent, the acetylcholine receptor was excluded from the Triton X-114 micelles. The structural implications of this result are discussed.
D000818:Animals; D004557:Electric Organ / Q000032:analysis; D066298:In Vitro Techniques; D017830:Octoxynol; D011092:Polyethylene Glycols; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000302:isolation & purification*; D014101:Torpedo / Q000378:metabolism
D011950:Receptors, Cholinergic; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40