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

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

doi:10.1016/S0141-0229(01)00352-0

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

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

Research output: Contribution to journal › Article › Research › peer-review

10 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	99-103
Journal	Enzyme and Microbial Technology
Volume	29
Issue number	1
DOIs	https://doi.org/10.1016/S0141-0229(01)00352-0
Publication status	Published - 5 Jul 2001

Keywords

Contaminants
MALDI-TOF MS
Monitoring expression
Protein purification
Recombinant protein

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10.1016/S0141-0229(01)00352-0

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title = "Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry",

abstract = "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. {\textcopyright} 2001 Elsevier Science Inc.",

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AU - Villanueva, Josep

AU - Canals, Francesc

AU - Querol, Enrique

AU - Avilés, Francesc X.

PY - 2001/7/5

Y1 - 2001/7/5

N2 - 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.

AB - 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.

KW - Contaminants

KW - MALDI-TOF MS

KW - Monitoring expression

KW - Protein purification

KW - Recombinant protein

U2 - 10.1016/S0141-0229(01)00352-0

DO - 10.1016/S0141-0229(01)00352-0

M3 - Article

SN - 0141-0229

VL - 29

SP - 99

EP - 103

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 1

ER -

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

Abstract

Keywords

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