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

Sandra Camprubí, Marc Bruguera, Francesca Canalias

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9 Citations (Scopus)

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™ 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. © 2006 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)134-139
JournalInternational Journal of Biological Macromolecules
Volume38
DOIs
Publication statusPublished - 30 Mar 2006

Keywords

  • Expanded bed adsorption
  • Immobilized metal affinity
  • Recombinant streptolysin O

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