title: Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry.
abstract: 1Samples 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.
authors: Institut de Biologia Fonamental and Departament de Bioquímica, Universitat Autònoma de Barcelona, 08193, Bellaterra (Barcelona), Spain
authors: J
authors: J
authors: Villanueva
authors: F
authors: F
authors: Canals
authors: E
authors: E
authors: Querol
authors: F X.
authors: FX
authors: Avilés