作者: Zhu Xiaoshan , Meng Fanping , He Donghai
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摘要: The brain acetylcholinesterase (AChE, EC 3.1.1.7) from Hexagrammos otakii is purified by affinity chromatography. specific activity of the enzyme 63.136 U/mg protein. optimal pH 8.0 and temperature 35℃. SDS-PAGE analysis preparation shows one band protein staining. ATCh observed to be hydrolyzed this but BTCh not. An exceeded substrate can inhibit enzyme. In addition, it inhibited BW284C51 (a selective inhibitor for AChE) not iso-OMPA [a butyrylcholinesterase (BuChE,EC 3.1.1.8)]. Thus, confirmed a true AChE.