摘要
金属螯合亲和层析是近 2 0年发展起来的一项新型分离技术。它以配基简单、吸附量大、分离条件温和、通用性强等特点 ,逐渐成为分离纯化蛋白质等生物工程产品最有效的技术之一。本文从单组分蛋白质入手 ,考查了 pH值、铵离子浓度、不同铵盐等对蛋白质洗脱的影响 ,并进行了分析。还对不同的金属螯合柱和不同性质蛋白质的洗脱性能进行了研究 ,比较了不同金属离子与蛋白质亲和力的区别 ,为实际体系的分离研究打下了基础。
Immobilized metal ion affinity chromatography (IMAC) has shown promise of isolating desired proteins from a mixture based on their difference of affinity for chelated metal ions.With its technological superiority,such as large adsorption capacity,mild separation condition,simple ligands and wide applications,IMAC has become powerful tool for biotechnological products separation,such as proteins,amino acids and gene products. In spite of many sophisticated applications for IMAC,the theoretical analysis of Immobilized metal chromatography has remained insufficient.In this paper,the eluted efficiencies of bovine serum albumin (BSA) in a single\|component system under different elution conditions are studied.The effects of several elution factors,such as pH value,ammonium concentration and anion species on protein separation are studied.Comparing the elution data of BSA in IDA Cu and IDA Zn columns,the different ability of affinity between metal ions and proteins is found.In addition,the elution behaviors of different proteins are investigated.This work facilitates the further research in separation of real systems.
出处
《生物工程学报》
CAS
CSCD
北大核心
2000年第4期495-499,共5页
Chinese Journal of Biotechnology
关键词
金属螯合亲和层析
分离
纯化
蛋白质
生物产品
Immobilized metal ion affinity chromatograph(IMAC), bovine serum albumin(BSA), hemoglobin, separation
