We introduce a matrix-assisted laser desorption ionization-Fourier transform ion cyclotron resonance (MALDI-FT-ICR) method for quantitative peptide profiling, using peak height as a measure for abundance. Relative standard deviations in peak height of peptides spiked over 3 orders of magnitude in concentration were below 10% and allowed for accurate comparisons between multiple sclerosis and controls. Application on a set of 163 cerebrospinal fluid (CSF) samples showed significantly differential abundant peptides, which were subsequently identified into proteins (e.g., chromogranin A, clusterin, and complement C3). © 2009 American Chemical Society.

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doi.org/10.1021/pr8010155, hdl.handle.net/1765/16460
Journal of Proteome Research
Erasmus MC: University Medical Center Rotterdam

Stoop, M., Dekker, L., Titulaer, M., Lamers, R. J. A. N., Burgers, P., Smitt, P., … Hintzen, R. (2009). Quantitative matrix-assisted laser desorption ionization-fourier transform ion cyclotron resonance (MALDI-FT-ICR) peptide profiling and identification of multiple-sclerosis-related proteins. Journal of Proteome Research, 8(3), 1404–1414. doi:10.1021/pr8010155