黄姑鱼肌肉胆碱酯酶的纯化及其某些性质

被引:13
作者
施善平
张景园
机构
[1] 中国科学院上海生物化学研究所
关键词
黄姑鱼; 亲和层析; 底物浓度; 底物抑制作用; 肌肉组织; 肌组织; 动物组织; 酶活力; 酶活性; 胆碱酯酶;
D O I
暂无
中图分类号
学科分类号
摘要
用亲和层析方法纯化了黄姑鱼(Nibea albiflora)肌肉胆碱酯酶。结合在膜上的胆碱酯酶用两种非离子型表面活性剂的混合液抽提、硫酸铵分级沉淀、再经一次亲和层析,共提纯11,800倍,最高比活力达2180活力单位/毫克蛋白,总活力回收约20%。纯化后的酶用聚丙烯酰胺凝胶电泳,除部分酶蛋白留在原点外,在凝胶内为单一蛋白染色区带,具有酶活力。SephadexG-200凝胶过滤得两个酶活力峰。亲和吸附剂在八个月内反复使用近20次,性能不变。对酶的一般性质作了初步的研究。根据酶的底物专一性、受真性酶专一性抑制剂抑制作用的敏感性及过量底物抑制作用的存在,可以认为黄姑鱼肌肉胆碱酯酶基本上具有真性酶的特征。
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页码:9 / 16
页数:8
相关论文
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