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使用串联径向流离子交换柱色谱法快速纯化重组蛋白。

Rapid purification of a recombinant protein using tandem radial flow ion-exchange column chromatography.

作者信息

McCartney J E

机构信息

Creative BioMolecules, Inc., Hopkinton, MA 01748.

出版信息

Biotechniques. 1991 Nov;11(5):648-9.

PMID:1804256
Abstract

Tandem radial flow anion- and cation-exchange columns were used to partially purify and concentrate a dilute recombinant protein that had been refolded in vitro after production as insoluble inclusion bodies in E. coli. The refolded sample was first passed through a Q-Sepharose Fast Flow column in order to remove the majority of E. coli contaminating proteins and endotoxins, then purified on an S-Sepharose Fast Flow column connected to the outlet of the Q-Sepharose column. This tandem arrangement enabled the rapid processing of multiple preparations of refolded material during production method development.

摘要

串联径向流阴离子和阳离子交换柱用于部分纯化和浓缩一种稀释的重组蛋白,该蛋白在大肠杆菌中作为不溶性包涵体产生后,已在体外进行了重折叠。重折叠后的样品首先通过Q-Sepharose Fast Flow柱,以去除大部分大肠杆菌污染蛋白和内毒素,然后在连接到Q-Sepharose柱出口的S-Sepharose Fast Flow柱上进行纯化。这种串联配置使得在生产方法开发过程中能够快速处理多份重折叠材料的制剂。

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