Abstract
The ability to combine a selective capture strategy with on chip MALDI-TOF analysis allows for rapid, sensitive analysis of a variety of different analytes. In this overview a series of applications of capture enhanced laser desorption ionization time of flight (CELDI-TOF) mass spectrometry are described. The key feature of the assay is an off-chip capture step that utilizes high affinity bacterial binding proteins to capture a selected ligand. This allows large volumes of sample to be used and provides for a concentration step prior to transfer to a gold chip for traditional mass spectral analysis. The approach can also be adapted to utilize specific antibody as the basis of the capture step. The direct and indirect CELDI-TOF assays are rapid, reproducible and can be a valuable proteomic tool for analysis of low abundance molecules present in complex mixtures like blood plasma.
Keywords: CELDI-TOF capture-enhanced laser desorption ionization time of flight mass spectroscopy, IdeS, Immunoglobulin G: albumin, cysteine proteases
Current Proteomics
Title: Novel Sample Preparation for Mass Spectral Analysis of Complex Biological Samples
Volume: 7 Issue: 2
Author(s): Eric A. Porsch, Cecelia A. Shertz and Michael D. Boyle
Affiliation:
Keywords: CELDI-TOF capture-enhanced laser desorption ionization time of flight mass spectroscopy, IdeS, Immunoglobulin G: albumin, cysteine proteases
Abstract: The ability to combine a selective capture strategy with on chip MALDI-TOF analysis allows for rapid, sensitive analysis of a variety of different analytes. In this overview a series of applications of capture enhanced laser desorption ionization time of flight (CELDI-TOF) mass spectrometry are described. The key feature of the assay is an off-chip capture step that utilizes high affinity bacterial binding proteins to capture a selected ligand. This allows large volumes of sample to be used and provides for a concentration step prior to transfer to a gold chip for traditional mass spectral analysis. The approach can also be adapted to utilize specific antibody as the basis of the capture step. The direct and indirect CELDI-TOF assays are rapid, reproducible and can be a valuable proteomic tool for analysis of low abundance molecules present in complex mixtures like blood plasma.
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Cite this article as:
A. Porsch Eric, A. Shertz Cecelia and D. Boyle Michael, Novel Sample Preparation for Mass Spectral Analysis of Complex Biological Samples, Current Proteomics 2010; 7 (2) . https://dx.doi.org/10.2174/157016410791330589
DOI https://dx.doi.org/10.2174/157016410791330589 |
Print ISSN 1570-1646 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6247 |
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