Purification of recombinant histidine-tag streptolysin O using immobilized metal affinity expanded bed adsorption (IMA-EBA)

International Journal of Biological Macromolecules
Sandra CamprubíFrancesca Canalias

Abstract

In this report, we describe the recombinant SLO expression as a fusion protein with a C-terminal hexahistidine tag and its purification using immobilized metal affinity expanded bed adsorption (STREAMLINE(trade mark) Chelating). In order to facilitate downstream processing of the purification, an efficient fermentation process was developed focusing on the achievement of high yields of soluble protein. The purification strategy resulted in a 40% recovery of active recombinant SLO and the protein was purified eight-fold. SDS-PAGE and Western-blot analysis of the purified protein revealed the presence of a 75 Mr form, which was the estimated relative Mass of the recombinant SLO.

References

Feb 19, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·S GibertX Santarelli
Feb 22, 2005·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Annelise SahinXavier Santarelli

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Citations

Nov 21, 2007·Protein Expression and Purification·Nuoyan ZhengQi Xie
Apr 5, 2007·Nature Protocols·Berend TolnerKerry A Chester

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