%0 Journal Article
%T Immobilized Ni2+-IDA Metal Chelating Affinity Membrane Chroma-tography for Purification of Commercial Human Serum Albumin<br>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
%A YANG Li
%A JlA Ling-yun
%A ZOU Han-fa
%A ZHNAG Yu-kui
%A <br>杨利
%A 贾凌云
%A 邹汉法
%A 张玉奎
%J 生物工程学报
%D 2000
%I 
%X 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.
%K Affinity chromatography
%K membrane
%K human scram albumin
%K purification
%K metal chelating<br>亲和色谱，膜，人血清白蛋白，纯化，金属螯合
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=9F824F4419BFBA52&yid=9806D0D4EAA9BED3&vid=7801E6FC5AE9020C&iid=CA4FD0336C81A37A&sid=67969BA850333433&eid=E44E40A2398D4F2A&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=5&reference_num=15