IDA型固定化镍离子金属螯合亲和膜色谱对人血清白蛋白的分离纯化

Immobilized Ni^(2+)-IDA Metal Chelating Affinity Membrane Chroma tography for Purification of Commercial Human Serum Albumin

采用自制的固定化镍离子亚氨二乙酸(IDA)型复合纤维素金属螯合膜色谱对药用人血清白蛋白的进一步纯化进行了研究。考察了pH对HAS吸附效果的影响。经一步纯化,商品药用HSA中的许多杂蛋白可被除去,经毛细管电泳分析,纯度与Sigma公司的电泳纯HSA相当,回收率可达85%以上。纯化蛋白液中的镍离子经过自制的N,N,N′三羧甲基乙二胺(TED)型螯合柱处理后可较好地除去。

Further purification of commercial human serum albumin was studied on immobilized Ni 2+ IDA composite membrane cartridge. Effect of pH on HSA binding capacity was examined. A lot of impurities in the commercial HSA had been removed by a single step purification with a recovery of more than 85% of the protein bound on membrane cartridge. The purified HSA was of comparable purity of that from Sigma company analyzed by capillary electrophoresis. The nickel ion retained in the protein solution could be removed efficiently with the N,N,N' tris (carboxymethyl) ethylenediamine chelating membrane cartridge.