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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 Ni2+-IDA Metal Chelating Affinity Membrane Chroma tography for Purification of Commercial Human Serum Albumin

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【作者】 杨利贾凌云邹汉法张玉奎

【Author】 YANG Li JIA Ling yun ZOU Han fa ZHNAG Yu kui (National Chromatographic R & A Center, Dalian Institute of Chemical Physics, The Chinese Academy of Sciences, Dalian 116011)

【机构】 中国科学院大连化学物理研究所国家色谱研究分析中心!大连116011

【摘要】 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。

【Abstract】 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.

【基金】 国家自然科学基金!资助项目 ( 2 96 3 5 0 10 )
  • 【文献出处】 生物工程学报 ,CHINESE JOURNAL OF BIOTECHNOLOGY , 编辑部邮箱 ,2000年01期
  • 【分类号】Q814.9
  • 【被引频次】23
  • 【下载频次】554
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