METAL-ION CONCENTRATION, TIME, AND PH-DEPENDENCE OF METAL-ION BINDING TO A TRANSFERRIN METALLOPROTEIN AFFINITY-CHROMATOGRAPHY (MAMC) MATRIX

被引：4

作者：

CANNELL, KP ^{[1
]}

VINCENT, JB ^{[1
]}

机构：

[1] UNIV ALABAMA, DEPT CHEM, TUSCALOOSA, AL 35487 USA

来源：

JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY | 1995年 / 64卷 / 01期

关键词：

TRANSFERRIN; CONALBUMIN; ADSORPTION ISOTHERMS;

D O I：

10.1002/jctb.280640115

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The adsorption of transition metal, lanthanide, and actinide ions to ovotransferrin (conalbumin) immobilized to sepharose (via the cyanogen bromide method) has been examined. Adsorption of ions as a function of time and adsorption isotherms at pH 8 have been determined and analyzed using the Freundlich model. Distribution coefficients between the pH values 2 and 9 have been measured. The results indicate that immobilization of the protein has little effect on its interactions with metal ions compared with the protein in solution, an important prerequisite for use of this matrix in metalloprotein affinity metal chromatography (MAMC).

引用

页码：96 / 100

页数：5

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