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Separate recombinant antibacterial peptide with immobilized metal-chelated affinity chromatography membranes.

文献类型: 外文期刊

作者: Wei, Q 1 ; Yao, RH 2 ; Bao, SX 2 ;

作者机构: 1.S China Univ Technol, Dept Bioengn, Guangzhou 510641, Peoples R China

2.S China Univ Technol, Dept Bioengn, Guangzhou 510641, Peoples R China; Chinese Acad Trop Agr Sci, Biotechnol Natl Key Lab, Haikou 571101, Peoples R China

关键词: affinity chromatography;affinity membrane;antibacterial peptide

期刊名称:PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS ( 影响因子:0.351; 五年影响因子:0.272 )

ISSN: 1000-3282

年卷期: 2000 年 27 卷 4 期

页码:

收录情况: SCI

摘要: Immobilized metal-chelated affinity chromatography (IMAC) membranes were prepared for separating a recombinant fusion antibacterial peptide, which carried a polyhistidine sequence (HIS6-tag) at the N-terminus. Low bleeding of metal ion was achieved. It was proved that the properties of IMAC membranes were better than conventional chelating sepharose fast flow column. The fractionation of recombinant proteins that carry a polyhistidine tag is currently perhaps the most promising application of IMAC.

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