Extraction of peripheral proteins from nicotinic acetylcholine receptor-enriched membranes.
The solubilisation of membrane proteins from nicotinic acetylcholine receptor-enriched membranes from the electric organ of Torpedo marmorata was studied. Chaotropic ions were shown to be ineffective in extracting peripheral proteins from these membranes. Two different anhydrides, 2, 3-dimethylmaleic and 3,4,5,6-tetrahydrophthalic anhydride, released certain peripheral membrane proteins but not the integral receptor protein. Treatment of membranes containing greater than 3 nmol alpha-bungarotoxin binding sites per mg protein with anhydride resulted in a 43 kDa polypeptide as the major constituent of the solubilised material. The nature of the 43 kDa polypeptide is discussed. Gentle anhydride treatment did not change the alpha-bungarotoxin and carbamoylcholine binding properties of the receptor.
D000818:Animals; D002038:Bungarotoxins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D004557:Electric Organ / Q000378:metabolism*; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D011950:Receptors, Cholinergic / Q000302:isolation & purification*; D011978:Receptors, Nicotinic / Q000302:isolation & purification* / Q000378:metabolism; D014101:Torpedo
D002038:Bungarotoxins; D008565:Membrane Proteins; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic