PURIFICATION AND PROPERTIES OF THE MEMBRANE-BOUND ACETYLCHOLINESTERASE FROM ADULT RAT BRAIN

Publisher Summary This chapter discusses a study to examine the purification and properties of the membrane-bound acetyicholinesterase from adult rat brain. The Triton X-l00 soluble acetylcholine esterase (AChE) from adult rat brain was purified to homogeneity using sequential affinity chromatography on Concanavalin-A-Sepharose and on dimethyl-amino-ethyl-benzoicacid-Sepharose followed by DEAE-cellulose chromatography. The yield of the purified enzyme is higher than 50%. Gel filtration and sucrose density gradient centrifugation in the presence of Triton X-100 gives only one symmetrical peak, with a calculated molecular weight of 328,000. As SDS poliacrylamide gelelectrophoresis in the presence of mercaptoethanol gives only one band with a molecular weight of 74,000, a tetrameric structure can be postulated for the membrane-bound AChE from rat brain.