Sechi | Quantitative Proteomics by Mass Spectrometry | Buch | 978-1-58829-571-2 | sack.de

Buch, Englisch, 218 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 560 g

Reihe: Methods in Molecular Biology

Sechi

Quantitative Proteomics by Mass Spectrometry


2007
ISBN: 978-1-58829-571-2
Verlag: Humana Press

Buch, Englisch, 218 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 560 g

Reihe: Methods in Molecular Biology

ISBN: 978-1-58829-571-2
Verlag: Humana Press


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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Weitere Infos & Material


Acrylamide—A Cysteine Alkylating Reagent for Quantitative Proteomics.- Using Stable Isotope Tagging and Mass Spectrometry to Characterize Protein Complexes and to Detect Changes in Their Composition.- Stable Isotope Labeling by Amino Acids in Cell Culture for Quantitative Proteomics.- Quantitative Proteomics of Mouse Brain and Specific Protein-Interaction Studies Using Stable Isotope Labeling.- The Absolute Quantification Strategy.- Quantification of Proteins and Metabolites by Mass Spectrometry Without Isotopic Labeling.- The Use of a Quantitative Cysteinyl-Peptide Enrichment Technology for High-Throughput Quantitative Proteomics.- An Isotope Coding Strategy for Proteomics Involving Both Amine and Carboxyl Group Labeling.- Proteolytic Labeling With 18O for Comparative Proteomics Studies.- Tandem Mass Spectrometry in the Detection of Inborn Errors of Metabolism for Newborn Screening.- Absolute Quantification of Specific Proteins in Complex Mixtures Using Visible Isotope-Coded Affinity Tags.- Computational Analysis of Quantitative Proteomics Data Using Stable Isotope Labeling.- Quantitative Proteomic Analysis of Mammalian Organisms Using Metabolically Labeled Tissues.- Quantitative Proteomic Analysis of Phosphotyrosine-Mediated Cellular Signaling Networks.



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