Mild conditions for releasing mono and bis-biotinylated macromolecules from immobilized streptavidin

被引：11

作者：

Nguyen, GH

Milea, JS

Rai, A

Smith, CL

机构：

[1] Mol Biol Res Lab, Boston, MA 02215 USA

[2] Boston Univ, Dept Biomed Engn, Boston, MA 02215 USA

[3] Dept Biol, Boston, MA 02215 USA

[4] Dept Pharmacol, Boston, MA 02215 USA

来源：

BIOMOLECULAR ENGINEERING | 2005年 / 22卷 / 04期

关键词：

streptavidin; biotin; biotinylated DNA;

D O I：

10.1016/j.bioeng.2005.02.003

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The high affinity (k(d) = similar to 10(-15) M) of streptavidin and avidin for biotin is key to a large number of biological applications and is essentially irreversible unless the complex is exposed to harsh conditions (e.g. heat (100 degrees C for 10 min)), detergents, and/or denaturants which damage macromolecules. Thus, high binding affinity becomes a disadvantage when a biotinylated target must be released for further processing. This work describes relatively mild conditions that release biotin and mono- and bis-biotinylated macromolecules from immobilized streptavidin on monodispersed magnetic beads. (C) 2005 Elsevier B.V. All rights reserved.

引用

页码：147 / 150

页数：4

共 17 条

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