Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions

We compared coupling approaches of SPR to LC-MS and ProteinChip™-based mass spectrometry (SELDI™) as a means of identifying proteins captured on DNA surfaces. The approach we outline has the potential to allow multiple, quantitative analysis of macromolecular interactions followed by rapid mass spec...

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Bibliographic Details
Published inNucleic acids research Vol. 35; no. 6; p. e39
Main Authors Bouffartigues, Emeline, Leh, Hervé, Anger-Leroy, Marielle, Rimsky, Sylvie, Buckle, Malcolm
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.03.2007
Oxford Publishing Limited (England)
Subjects
Bacterial Proteins
Bacterial Proteins - analysis
Biochemistry, Molecular Biology
Chromatography, Liquid
DNA-Binding Proteins
DNA-Binding Proteins - analysis
Life Sciences
Methods Online
Nuclear Proteins
Nuclear Proteins - analysis
Protein Array Analysis
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Surface Plasmon Resonance
Surface Plasmon Resonance - methods
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Summary:We compared coupling approaches of SPR to LC-MS and ProteinChip™-based mass spectrometry (SELDI™) as a means of identifying proteins captured on DNA surfaces. The approach we outline has the potential to allow multiple, quantitative analysis of macromolecular interactions followed by rapid mass spectrometry identification of retained material.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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PMCID: PMC1874600
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkm030