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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
引用本文:杨利,贾凌云,邹汉法,张玉奎.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[J].生物工程学报,2000,16(1):74-77.
作者姓名:杨利  贾凌云  邹汉法  张玉奎
作者单位: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
基金项目:国家自然科学基金资助项目(29635010)。
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HAS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HAS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。

关 键 词:亲和色谱,膜,人血清白蛋白,纯化,金属螯合
文章编号:1000-3061(2000)01-0074-04
修稿时间:1998-10-14

Immobilized Ni2+-IDA Metal Chelating Affinity Membrane Chroma-tography for Purification of Commercial Human Serum Albumin
YANG Li,JlA Ling-yun,ZOU Han-fa,ZHNAG Yu-kui.Immobilized Ni2+-IDA Metal Chelating Affinity Membrane Chroma-tography for Purification of Commercial Human Serum Albumin[J].Chinese Journal of Biotechnology,2000,16(1):74-77.
Authors:YANG Li  JlA Ling-yun  ZOU Han-fa  ZHNAG Yu-kui
Institution:YANG Li ,JlA 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)
Abstract:Further purification of commercial human serum albumin was studied on immobilized Ni2+-IDA composite membrane cartridge. Effect of pH on HAS binding capacity was examined. A lot of impurities in the commercial HAS had been removed by a single step purification with a recovery of more than 85 % of the protein bound on membrane car tridge. The purified HAS 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.
Keywords:Affinity chromatography  membrane  human scram albumin  purification  metal chelating
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