Overview

 Glycosylation is the most abundant post-translational modification of proteins.  Estimates vary widely, but a common assessment is that upwards of 50% of eukaryotic proteins are modified by some type of glycan. In Mass Spectrometry of Glycoproteins: Methods and Protocols, expert researchers in the field detail many of the methods that are now commonly used for glycoproteomics.  These methods and techniques include robust sample preparation techniques; advanced chromatographic strategies for improving dynamic range; state-of-the-art mass spectrometry instrumentation and associated ionization and fragmentation methods; and informatics tools used for identifying glycoproteins and characterizing the associated glycans. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.   Authoritative and practical, Mass Spectrometry of Glycoproteins: Methods and Protocol  is  an essential resource for those who work at the interface of glycobiology and mass spectrometry.

Full Product Details

Author:   Jennifer J. Kohler ,  Steven M. Patrie
Publisher:   Humana Press Inc.
Imprint:   Humana Press Inc.
Edition:   2013 ed.
Volume:   951
Dimensions:   Width: 17.80cm , Height: 2.60cm , Length: 25.40cm
Weight:   0.859kg
ISBN:  

9781627031455

ISBN 10:   1627031456
Pages:   339
Publication Date:   08 January 2013
Audience:   College/higher education ,  Professional and scholarly ,  Postgraduate, Research & Scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Active
Availability:   Manufactured on demand  
We will order this item for you from a manufactured on demand supplier.

Table of Contents

Introduction to Glycosylation and Mass Spectrometry.-Tandem Lectin Weak Affinity Chromatography (LWAC) for Glycoprotein Enrichment.-CSC Technology - Selective Labeling of Glycoproteins by Mild Oxidation to Phenotype Cells.-Use of Boronic Acid Nanoparticles in Glycoprotein Enrichment.-Incorporation of Unnatural Sugars for the Identification of Glycoproteins.-Characterization of Membrane-associated Glycoproteins using Lectin Affinity Chromatography and Mass Spectrometry.-Sialic Acid Capture-and-Release and LC-MSn Analysis of Glycopeptides.-In-Solution Digestion of Glycoproteins for Glycopeptide-Based Mass Analysis.-Nano-HPLC-MS of Glycopeptides Obtained After Non-specific Proteolysis.-Glycopeptide Enrichment for MALDI-TOF Mass Spectrometry Analysis by Hydrophilic Interaction Liquid Chromatography Solid Phase Extraction (HILIC SPE).-Separation and Identification of Glycoforms by Capillary Electrophoresis with Electrospray Ionization Mass Spectrometric Detection.-Structural Separations by Ion Mobility-MS for Glycomics and Glycoproteomics.-Quantitative Analysis of Glycoprotein Glycans.-Stable Isotope Labeling of N-glycosylated Peptides by Enzymatic Deglycosylation for Mass Spectrometry-based Glycoproteomics.-Approaches for Site Mapping and Quantification of O-linked Glycopeptides.-Glycan Profiling: Label-free Analysis of Glycoproteins.-Introduction to Informatics in Glycoprotein Analysis.-Software Tools for Glycan Profiling.-Quantitative Characterization of Glycoproteins in Neurodegenerative Disorders using iTRAQ.-Quantitative Proteomic Analysis of N-linked Glycoproteins in Human Tear Fluid.-Elucidation of N-glycosites Within Human Plasma Glycoproteins for Cancer Biomarker Discovery.-Characterizing the Glycosylation State of Therapeutic RecombinantGlycoproteins.

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