EVALUATION OF THE INTERACTION OF PROTEIN ALPHA-AMINO GROUPS WITH M(II) BY IMMOBILIZED METAL-ION AFFINITY-CHROMATOGRAPHY

被引：31

作者：

ANDERSSON, L

SULKOWSKI, E

机构：

[1] Biochemical Separation Centre, Biomedical Centre, University of Uppsala, S-751 23 Uppsala

来源：

JOURNAL OF CHROMATOGRAPHY | 1992年 / 604卷 / 01期

关键词：

D O I：

10.1016/0021-9673(92)85523-V

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The adsorption properties of various peptides and proteins, lacking histidyl groups, on immobilized Cu(II), Ni(II), Zn(II) and Co(II) ions are described; at pH 6 and below they were little retarded. At higher pH the retention became pronounced for iminodiacetate (IDA)-Cu(II) gel. This effect seems to be related to the presence of a terminal-alpha-amino group; in the absence of this group the retention of the protein was largely eliminated. At pH 8.5 a terminal-alpha-amino group is adsorbed as strongly as a histidyl group. IDA-Ni(II), IDA-Zn(H) and IDA-Co(II) gels display little or no attraction for the terminal-alpha-amino group of a protein.

引用

页码：13 / 17

页数：5

共 10 条

[1] PURIFICATION OF COMMERCIAL HUMAN-ALBUMIN ON IMMOBILIZED IDA-NI2+ [J].