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Title: Purification and isolation of choline acetyltransferase from the electric organ of Torpedo marmorata by affinity chromatography. Author: Raeber AJ, Riggio G, Waser PG. Journal: Eur J Biochem; 1989 Dec 22; 186(3):487-92. PubMed ID: 2606102. Abstract: Choline acetyltransferase (EC 2.3.1.6) catalyzes the synthesis of the neurotransmitter acetylcholine from acetylcoenzyme A and choline. It has been purified from the electric organ of Torpedo marmorata by a new double-affinity chromatography. Our rapid and specific purification procedure includes affinity chromatography on CoA-Sepharose and then a second affinity chromatography on the enzyme's inhibitor [2-[3-(2-ammonioethoxy)-benzoyl]ethyl]trimethylammonium bromide coupled to Sepharose via a six-carbon spacer arm. The final enzyme preparation has been purified 7300-fold to a specific activity of 73 mumol acetylcholine formed min-1 mg protein-1. The isolated enzyme gave a single band on disc polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The relative molecular mass was determined to be 68,300 +/- 2100.[Abstract] [Full Text] [Related] [New Search]