Quantitative proteomics by mass spectrometry / edited by Salvatore Sechi.

Contributor(s): Sechi, Salvatore, 1960-
Material type: TextTextSeries: Methods in molecular biology (Clifton, N.J.): v. 359.Publisher: Totowa, N.J. : Humana Press, ©2007Description: 1 online resource (x, 218 pages) : illustrationsContent type: text Media type: computer Carrier type: online resourceISBN: 9781597452557; 1597452556; 1280832738; 9781280832734Subject(s): Mass spectrometry -- Technique | Proteomics -- Methodology | Proteomics -- methods | Mass Spectrometry -- methods | Proteomics | Mass Spectrometry | Methods | Biochemistry | Chemistry Techniques, Analytical | Genomics | Investigative Techniques | Genetics | Chemistry | Analytical, Diagnostic and Therapeutic Techniques and Equipment | Computational Biology | Biological Science Disciplines | Natural Science Disciplines | Biology | Disciplines and Occupations | SCIENCE -- Life Sciences -- Biochemistry | Proteomics -- methods | Mass Spectrometry -- methods | Mass spectrometry -- Technique | Proteomics -- Methodology | Mass spectrometry -- Technique | Massenspektrometrie | Proteomanalyse | Quantitative Analyse | massaspectrometrie | mass spectrometry | eiwitexpressieanalyse | proteomics | Analytical Chemistry | Analytische chemieGenre/Form: Electronic books. | Aufsatzsammlung. Additional physical formats: Print version:: Quantitative proteomics by mass spectrometry.DDC classification: 572/.36 LOC classification: QP519.9.M3 | Q36 2007Other classification: Q510. 3 | WC 4170 | WD 5100 | CHE 828f | CHE 254f Online resources: Click here to access online
Contents:
Acrylamide: a cysteine alkylating reagent for quantitative proteomics / Illarion V. Turko and Salvatore Sechi -- Using stable isotope tagging and mass spectrometry to characterize protein complexes and to detect changes in their composition / Jeffrey A. Ranish, Marjorie Brand, and Ruedi Aebersold -- Stable isotope labeling by amino acids in cell culture for quantitative proteomics / Shao-En Ong and Matthias Mann -- Quantitative proteomics of mouse brain, and specific protein-interaction studies using stable isotope labeling / Toshitaka Sato, Yasushi Ishihama, and Yoshiya Oda -- The absolute quantification strategy: application to phosphorylation profiling of human separase serine 1126 / Scott A. Gerber [and others] -- Quantification of proteins and metabolites by mass spectrometry without isotopic labeling / Sushmita Mimi Roy and Christopher H. Becker -- The use of a quantitative cysteinyl-peptide enrichment technology for high-throughput quantitative proteomics / Tao Liu [and others].
An isotope coding strategy for proteomics involving both amine and carboxyl group labeling / Fred E. Regnier -- Proteolytic labeling with 18O for comparative proteomics studies: preparation of 18O-labeled peptides and the 18O/16O peptide mixture / Catherine Fenselau and Xudong Yao -- Tandem mass spectrometry in the detection of inborn errors of metabolism and newborn screening / Frantisěk Turecěk, C. Ronald Scott, and Michael H. Gelb -- Absolute quantification of specific proteins in complex mixtures using visible isotope-coded affinity tags / Yu Lu [and others] -- Computational analysis of quantitative proteomics data using stable isotope labeling / Michael J. MacCoss and Christine C. Wu -- Quantitative proteomic analysis of mammalian organisms using metabolically labeled tissues / Christine C. Wu, and Michael J. MacCoss -- Quantitative proteomic analysis of phosphotyrosine-mediated cellular signaling networks / Yi Zhang, Alejandro Wolf-Yadlin, and Forest M. White.
Summary: Quantitative Proteomics by Mass Spectrometry, from the Methods in Molecular Biology™ series, is a compendium of cutting-edge protocols for quantitative proteomics, and presents the most significant methods used in the field today. The focus on mass spectrometry (MS) is integral, as MS has, and will continue to be, an essential tool in proteomics for studying complex biological systems and human diseases. This volume, written and compiled by leading quantitative proteomic experts, is an indispensable resource in the search for novel biomarkers. Quantitative Proteomics by Mass Spectrometry presents several innovative MS quantitative procedures, including a variety of methods for introducing isotopic labels and quantifying post-translational modifications. Some of these methods include growing an organism in isotope-enriched media, performing trypsin proteolysis in the presence of 18O-water, reacting protein samples with isotopically labeled reagents, quantifying relative amount of proteins without the use of any isotopic labels. Attention is also given to state-of-the-art techniques for the characterization of the phosphoproteome and tandem MS for detection of inborn errors of metabolism. Specifically, the procedure for determinations of enzymatic activity could be used for large-scale screening of newborns. The protocols in this volume expand both the breadth and depth of readily available methods for quantitative proteomic researchers using MS.
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Includes bibliographical references and index.

Acrylamide: a cysteine alkylating reagent for quantitative proteomics / Illarion V. Turko and Salvatore Sechi -- Using stable isotope tagging and mass spectrometry to characterize protein complexes and to detect changes in their composition / Jeffrey A. Ranish, Marjorie Brand, and Ruedi Aebersold -- Stable isotope labeling by amino acids in cell culture for quantitative proteomics / Shao-En Ong and Matthias Mann -- Quantitative proteomics of mouse brain, and specific protein-interaction studies using stable isotope labeling / Toshitaka Sato, Yasushi Ishihama, and Yoshiya Oda -- The absolute quantification strategy: application to phosphorylation profiling of human separase serine 1126 / Scott A. Gerber [and others] -- Quantification of proteins and metabolites by mass spectrometry without isotopic labeling / Sushmita Mimi Roy and Christopher H. Becker -- The use of a quantitative cysteinyl-peptide enrichment technology for high-throughput quantitative proteomics / Tao Liu [and others].

An isotope coding strategy for proteomics involving both amine and carboxyl group labeling / Fred E. Regnier -- Proteolytic labeling with 18O for comparative proteomics studies: preparation of 18O-labeled peptides and the 18O/16O peptide mixture / Catherine Fenselau and Xudong Yao -- Tandem mass spectrometry in the detection of inborn errors of metabolism and newborn screening / Frantisěk Turecěk, C. Ronald Scott, and Michael H. Gelb -- Absolute quantification of specific proteins in complex mixtures using visible isotope-coded affinity tags / Yu Lu [and others] -- Computational analysis of quantitative proteomics data using stable isotope labeling / Michael J. MacCoss and Christine C. Wu -- Quantitative proteomic analysis of mammalian organisms using metabolically labeled tissues / Christine C. Wu, and Michael J. MacCoss -- Quantitative proteomic analysis of phosphotyrosine-mediated cellular signaling networks / Yi Zhang, Alejandro Wolf-Yadlin, and Forest M. White.

Print version record.

Quantitative Proteomics by Mass Spectrometry, from the Methods in Molecular Biology™ series, is a compendium of cutting-edge protocols for quantitative proteomics, and presents the most significant methods used in the field today. The focus on mass spectrometry (MS) is integral, as MS has, and will continue to be, an essential tool in proteomics for studying complex biological systems and human diseases. This volume, written and compiled by leading quantitative proteomic experts, is an indispensable resource in the search for novel biomarkers. Quantitative Proteomics by Mass Spectrometry presents several innovative MS quantitative procedures, including a variety of methods for introducing isotopic labels and quantifying post-translational modifications. Some of these methods include growing an organism in isotope-enriched media, performing trypsin proteolysis in the presence of 18O-water, reacting protein samples with isotopically labeled reagents, quantifying relative amount of proteins without the use of any isotopic labels. Attention is also given to state-of-the-art techniques for the characterization of the phosphoproteome and tandem MS for detection of inborn errors of metabolism. Specifically, the procedure for determinations of enzymatic activity could be used for large-scale screening of newborns. The protocols in this volume expand both the breadth and depth of readily available methods for quantitative proteomic researchers using MS.

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