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Article: Technical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application

TitleTechnical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and application
Authors
KeywordsMatrix-Assisted Laser Desorption/Ionization Time-Of-Flight Mass Spectrometry
Nitrocellulose
Quantitative Proteomics
Reproducibility
Variation
Issue Date2004
Citation
Clinical Proteomics, 2004, v. 1 n. 3-4, p. 259-270 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/184289
ISSN
2015 Impact Factor: 3.476
2015 SCImago Journal Rankings: 1.210
References

 

DC FieldValueLanguage
dc.contributor.authorPang, RTKen_US
dc.contributor.authorJohnson, PJen_US
dc.contributor.authorChan, CMLen_US
dc.contributor.authorKong, EKCen_US
dc.contributor.authorChan, ATCen_US
dc.contributor.authorSung, JJYen_US
dc.contributor.authorPoon, TCWen_US
dc.date.accessioned2013-07-04T06:10:50Z-
dc.date.available2013-07-04T06:10:50Z-
dc.date.issued2004en_US
dc.identifier.citationClinical Proteomics, 2004, v. 1 n. 3-4, p. 259-270en_US
dc.identifier.issn1542-6416en_US
dc.identifier.urihttp://hdl.handle.net/10722/184289-
dc.description.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.en_US
dc.languageengen_US
dc.relation.ispartofClinical Proteomicsen_US
dc.subjectMatrix-Assisted Laser Desorption/Ionization Time-Of-Flight Mass Spectrometryen_US
dc.subjectNitrocelluloseen_US
dc.subjectQuantitative Proteomicsen_US
dc.subjectReproducibilityen_US
dc.subjectVariationen_US
dc.titleTechnical evaluation of MALDI-TOF mass spectrometry for quantitative proteomic profiling: Matrix formulation and applicationen_US
dc.typeArticleen_US
dc.identifier.emailPang, RTK: rtkpang@hku.hken_US
dc.identifier.authorityPang, RTK=rp01761en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1385/CP:1:3-4:259en_US
dc.identifier.scopuseid_2-s2.0-24644507027en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-24644507027&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume1en_US
dc.identifier.issue3-4en_US
dc.identifier.spage259en_US
dc.identifier.epage270en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPang, RTK=7004376636en_US
dc.identifier.scopusauthoridJohnson, PJ=7405661637en_US
dc.identifier.scopusauthoridChan, CML=36096478600en_US
dc.identifier.scopusauthoridKong, EKC=36784056000en_US
dc.identifier.scopusauthoridChan, ATC=13404833700en_US
dc.identifier.scopusauthoridSung, JJY=35405352400en_US
dc.identifier.scopusauthoridPoon, TCW=7006151710en_US

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