Quantitative matrix-assisted laser desorption ionization-fourier transform ion cyclotron resonance (MALDI-FT-ICR) peptide profiling and identification of multiple-sclerosis-related proteins
2009-03-06
Article
volume 8, issue 3 pp 1404-1414.
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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.
Keywords
- adult
- article
- female
- human
- male
- major clinical study
- priority journal
- controlled study
- matrix assisted laser desorption ionization time of flight mass spectrometry
- multiple sclerosis
- Cerebrospinal fluid
- Multiple sclerosis
- enzyme linked immunosorbent assay
- amino acid sequence
- Innate immunity
- Proteomics
- Clinically isolated syndrome
- Differentially abundant peptides
- chromogranin A
- clusterin
- complement component C3
- ion cyclotron resonance mass spectrometry
- matrix assisted laser desorption ionization fourier transform ion cyclotron resonance
- peptide analysis
