UM
Technical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application
Pang R.T.K.2; Johnson P.J.3; Chan C.M.L.1; Kong E.K.C.1; Chan A.T.C.1; Sung J.J.Y.2; Poon T.C.W.2
2004-09-01
Source PublicationClinical Proteomics
ISSN15426416
Volume1Issue:3-4Pages:259-270
AbstractMatrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) has been recently used to identify disease markers by directly profiling and quantifying the peptide/proteins in biological samples under different physiological or experimental conditions. The information of reproducibility of such quantitative profiling method has not been available. It is important to evaluate and reduce error from technical variation. In this study, an unbiased signal acquisition strategy was used to evaluate the effects of three sample-matrix spotting methods and two matrix chemicals, α-cyano-4-hydroxycin-namic acid (CHCA) and sinapinic acid, on the reproducibility of the peptide/protein signal intensities. The sandwich spotting method using 0.1% nitrocellulose coating film and CHCA gave the best quantitative results for the standard peptides and proteins with mass <66.5 kDa. The normalized signal intensities of the standard peptides and proteins were directly proportional to their concentrations with intra-assay (within-day) coefficient of variations (CVs) ranging from 6.5% to 17%. When analyzing serum peptides <6000 m/z, the interassay (between-days) CVs of all the evaluated peptide peaks were <15%. These data indicate that with the right MS analysis conditions, MALDI-TOF MS appears to be a feasible tool for directly profiling and quantifying the peptide/proteins in biological samples. Copyright © Humana Press Inc. All rights of any nature whatsoever are reserved.
KeywordMatrix-assisted laser desorption/ionization time-of-flight mass spectrometry Nitrocellulose Quantitative proteomics Reproducibility Variation
DOI10.1385/CP:1:3-4:259
URLView the original
Language英語
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Document TypeJournal article
CollectionUniversity of Macau
Affiliation1.Prince of Wales Hospital Hong Kong
2.Chinese University of Hong Kong
3.University of Birmingham
Recommended Citation
GB/T 7714
Pang R.T.K.,Johnson P.J.,Chan C.M.L.,et al. Technical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application[J]. Clinical Proteomics,2004,1(3-4):259-270.
APA Pang R.T.K.,Johnson P.J.,Chan C.M.L.,Kong E.K.C.,Chan A.T.C.,Sung J.J.Y.,&Poon T.C.W..(2004).Technical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application.Clinical Proteomics,1(3-4),259-270.
MLA Pang R.T.K.,et al."Technical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application".Clinical Proteomics 1.3-4(2004):259-270.
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