鲅鱼脑组织AChE的分离纯化及某些生化性质

Purification and Partial Biochemical Characterization of Acetylcholinesterase from Scomberomorus Niphonius(Cuvier)

采用亲和层析法对鲅鱼[Scomberomorus niphonius （Cuvier）]脑组织的胆碱酯酶[acetylcholinesterase （ACHE），EC3．1．1．7]进行分离纯化，然后对其进行底物特异性、过量底物抑制效应和抑制剂选择性检验。结果证实：该酶为乙酰胆碱酯酶（ACHE），其最大比活力为297．82μmol／（min·mg），最佳pH范围在7．0～8．0之间，最佳温度为30℃。此酶经过SDS—PAGE呈一条带，表明其纯度达电泳纯。

The brain acetylcholinesterase （ACHE, EC 3.1.1.7） from Scomberomorus niphonius （Cuvier） was purified by affinity chromatography. ATCh is observed to be hydrolyzed by this purified enzyme but BTCh not. And exceeded substrate can inhibit the activity of this enzyme. In addition, it can be inhibited by BW284C51 （a selective inhibitor for ACHE）and not by iso-OMPA [a selective inhibitor for butyrylcholinesterase （BuChE,EC 3.1.1.8）]. Thus, the purified enzyme is confirmed to be a true ACHE. The specific activity of the enzyme is 297.82 tamol/（min · mg）. The optimal pH of the enzyme lies between 7.0- 8.0 and the optimal temperature is 30 ℃. After the SDS-PAGE analysis, the purified enzyme preparation shows one band by protein staining.