Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry

Josep Villanueva, Francesc Canals, Enrique Querol, Francesc X. Avilés

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10 Citations (Scopus)


Samples coming from biologic sources usually contain several contaminants that interfere seriously with Mass Spectrometry (MS) measurements. In this paper we report the application of MALDI-TOF MS to monitor recombinant protein expression and purification. The technique is based on the use of a C18 resin to clean and concentrate proteins in batch. The utility of this method is demonstrated for samples coming from different bacterial cultures expressing secreted and intracellular proteins ranging from 4 to 53 kDa. MALDI-TOF MS of peptide and proteins can be accomplished directly from complex bacterial cultures or from any purification step in a few minutes using the conventional stainless steel sample targets, allowing for a nearly instantaneous monitoring of the nature and integrity of recombinant expression products. © 2001 Elsevier Science Inc.
Original languageEnglish
Pages (from-to)99-103
JournalEnzyme and Microbial Technology
Issue number1
Publication statusPublished - 5 Jul 2001


  • Contaminants
  • Monitoring expression
  • Protein purification
  • Recombinant protein


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