Yang L, Jia L Y, Zou H F, Zhnag Y K
National Chromatographic R & A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences.
Sheng Wu Gong Cheng Xue Bao. 2000 Jan;16(1):74-7.
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.
研究了在固定化镍离子-亚氨基二乙酸复合膜柱上对市售人血清白蛋白进行进一步纯化。考察了pH对人血清白蛋白结合容量的影响。通过一步纯化去除了市售人血清白蛋白中的大量杂质，膜柱上结合蛋白的回收率超过85%。经毛细管电泳分析，纯化后的人血清白蛋白纯度与Sigma公司的相当。用N，N，N'-三（羧甲基）乙二胺螯合膜柱可有效去除保留在蛋白质溶液中的镍离子。
