【摘要】 详细研究了亚氨基二乙酸（ＩＤＡ）在硅胶基质上键合的适宜条件，利用国产小颗粒大孔径硅胶（７μｍ，３０ｎｍ）制备了固定有Ｃｕ２＋，Ｎｉ２＋，Ｃｏ２＋，Ｚｎ２＋的金属螯合吸附剂，比较了蛋白质在金属螯合柱和裸柱上的保留特性，利用合成的Ｃｕ－ＩＤＡ－硅胶柱分离了来自牛血红细胞的超氧化物歧化酶（ＳＯＤ）。更多还原

【Abstract】 The appropriate conditions of bonding iminodiacetic acid(IDA) on silica matrix were studied in detail. These involve: the bonded amount of 0.75gIDA/g silica; reaction temperature 50 60℃; sodium carbonate buffer of initial pH 8.0 and reaction time 12h. The iminodiacetate substituted silica(IDA silica) and metal chelate adsorbents loading with Cu 2+ , Ni 2+ , Co 2+ and Zn 2+ were prepared by using the domestic small particle silica with wide pore(7μm, 30nm) at the proposed reaction conditions. The bonded density of iminodiacetate was about 23.4μmol per gramme of dry silica. After loading with Cu 2+ , Ni 2+ , Co 2+ and Zn 2+ , the adsorption capacity for lysozyme was 8.8 12.7mg per gramme of dry adsorbents. The retention characteristics of proteins were compared on the metal chelate column and the bare column. The effects of solution pH on the retention of protein were examined. The results showed that the interaction between the proteins and strong binding Cu column is mainly caused by coordination, and secondly by the electrostatic interaction; however, the interaction between proteins and stationary phase for weak binding Ni, Co and Zn column is contrary to Cu column. The superoxide dismutase(SOD) from bovine erythrocytes was isolated by the synthesized Cu IDA silica column and NH 3 competition elution manner. According to the determination of activity, the activity recovery of superoxide dismutase was greater than 74% and the specific activity was 4 590 U/(mg protein). Its purity increased up to 10 folds.更多还原