Fractionation of protein components of plasma membranes from the electric organ of Torpedo marmorata.
A procedure has been developed for the separation of intrinsic proteins of plasma membranes from the electric organ of Torpedo marmorata. (Na+ + K+)-ATPase, nicotinic acetylcholine receptor and acetylcholinesterase remained active after solubilization with the nonionic detergent dodecyl octaethylene glycol monoether (C12E8). These components could be separated by ion exchange chromatography on DEAE-Sephadex A-25. Fractions enriched in ouabain-sensitive K+-phosphatase or (Na+ + K+)-ATPase activity showed two bands in sodium dodecyl sulphate polyacrylamide gel electrophoresis corresponding to the alpha- and beta-subunits. The (Na+ + K+)-ATPase was shown to have immunological determinants in common with a 93 kDa polypeptide which copurified with the nicotinic acetylcholine receptor, also after solubilization in Triton X-100 and chromatography on Naja naja siamensis alpha-toxin-Sepharose columns. The data suggest that the alpha-subunit of (Na+ + K+)-ATPase associates with the acetylcholine receptor in the membranes of the electric organ.
D000110:Acetylcholinesterase / Q000302:isolation & purification; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism*; D004557:Electric Organ / Q000201:enzymology / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D011978:Receptors, Nicotinic / Q000302:isolation & purification; D000254:Sodium-Potassium-Exchanging ATPase / Q000302:isolation & purification; D014101:Torpedo
D008565:Membrane Proteins; D011978:Receptors, Nicotinic; D000110:Acetylcholinesterase; D000254:Sodium-Potassium-Exchanging ATPase