Capillary Electrophoresis Interfaced with a Mass Spectrometer (CE-MS): Technical Considerations and Applicability for Biomarker Studies in Animals

Author(s): Amaya Albalat, Holger Husi, Justyna Siwy, Jarlath E. Nally, Mark McLauglin, Peter D. Eckersall, William Mullen

Journal Name: Current Protein & Peptide Science

Volume 15 , Issue 1 , 2014

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Abstract:

Proteomics is a growing field that has the potential to be applied to many biology-related disciplines. However, the study of the proteome has proven to be very challenging due to its high level of complexity when compared to genome and transcriptome data. In order to analyse this level of complexity, high resolution separation of peptides/proteins are needed together with high resolution analysers. Currently, liquid chromatography and capillary electrophoresis (CE) are the two most widely used separation techniques that can be coupled on-line with a mass spectrometer (MS). In CE, proteins/ peptides are separated according to their size, charge and shape leading to high resolving power. Although further progress in the area of sensitivity, throughput and proteome coverage are expected, MS-based proteomics have developed to a level at which they are habitually applied to study a wide range of biological questions. The aim of this review is to present CE-MS as a proteomic analytical platform for biomarker research that could be used in farm animal and veterinary studies. This is a MS-analytical platform that has been widely used for biomarker research in the biomedical field but its application in animal proteomic studies is relatively novel. The review will focus on introducing the CE-MS platform and the primary considerations for its application to biomarker research. Furthermore, current applications but more importantly potential application in the field of farm animals and veterinary science will be presented and discussed.

Keywords: Biomarkers, CE-MS, farm animals, peptide profiling.

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Article Details

VOLUME: 15
ISSUE: 1
Year: 2014
Page: [23 - 35]
Pages: 13
DOI: 10.2174/1389203715666140221123920

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