APTAMER-BASED ALTERNATIVES TO THE CONVENTIONAL IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY FOR PURIFICATION OF HIS-TAGGED PROTEINS

被引：11

作者：

Lim, Hyun Kyung

Kim, Il-Hyun

Nam, Hye Yeon

Shin, Seonmi

Hah, Sang Soo ^{[1
,2
]}

机构：

[1] Kyung Hee Univ, Dept Chem, Seoul 130701, South Korea

[2] Kyung Hee Univ, Res Inst Basic Sci, Seoul 130701, South Korea

来源：

ANALYTICAL LETTERS | 2013年 / 46卷 / 03期

基金：

新加坡国家研究基金会;

关键词：

Affinity chromatography; Aptamer; His-tagged; PLATFORM; POLYMER; SENSOR;

D O I：

10.1080/00032719.2012.721105

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Aptamers are oligonucleotides or peptide molecules that are able to bind to their specific target molecules with high affinity via molecular recognition. In this study, we present development of aptamer-based affinity purification for His-tagged proteins for comparison of purification efficiency with the conventional Ni2+-based affinity chromatography. Thiol-functionalized aptamers able to specifically bind to His-tag were immobilized employing two crosslinking methods onto the surface of polystyrene resins. The resulting aptamer-anchored resins were successfully applied for purification of His-tagged proteins from complex E. coli and human cell lysates, respectively, and superior or at least comparable purification results to the conventional immobilized metal affinity chromatography were obtained via one-step purification.

引用

收藏

页码：407 / 415

页数：9

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