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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Detalles Bibliográficos
Autores principales: Bouffartigues, Emeline, Leh, Hervé, Anger-Leroy, Marielle, Rimsky, Sylvie, Buckle, Malcolm
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Methods Online
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1874600/
https://www.ncbi.nlm.nih.gov/pubmed/17287289
http://dx.doi.org/10.1093/nar/gkm030
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author Bouffartigues, Emeline
Leh, Hervé
Anger-Leroy, Marielle
Rimsky, Sylvie
Buckle, Malcolm
author_facet Bouffartigues, Emeline
Leh, Hervé
Anger-Leroy, Marielle
Rimsky, Sylvie
Buckle, Malcolm
author_sort Bouffartigues, Emeline
collection PubMed
description 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.
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spelling pubmed-18746002007-05-23 Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions Bouffartigues, Emeline Leh, Hervé Anger-Leroy, Marielle Rimsky, Sylvie Buckle, Malcolm Nucleic Acids Res Methods Online 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. Oxford University Press 2007-03 2007-02-07 /pmc/articles/PMC1874600/ /pubmed/17287289 http://dx.doi.org/10.1093/nar/gkm030 Text en © 2007 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Methods Online
Bouffartigues, Emeline
Leh, Hervé
Anger-Leroy, Marielle
Rimsky, Sylvie
Buckle, Malcolm
Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title_full Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title_fullStr Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title_full_unstemmed Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title_short Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
title_sort rapid coupling of surface plasmon resonance (spr and spri) and proteinchip™ based mass spectrometry for the identification of proteins in nucleoprotein interactions
topic Methods Online
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1874600/
https://www.ncbi.nlm.nih.gov/pubmed/17287289
http://dx.doi.org/10.1093/nar/gkm030
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