?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.
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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.
This comprehensive new resource in Springers Methods in Molecular Biology series features contributions from leading researchers who provide expert advice and reproducible, cutting-edge protocols for examining glycoproteins through mass spectrometry.
1. Introduction to Glycosylation and Mass Spectrometry
Steven M. Patrie, Michael J. Roth and Jennifer J. Kohler
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Part I Enrichment and Isolation Methods
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2. Tandem Lectin Weak Affinity Chromatography (LWAC) for Glycoprotein Enrichment
Zhi Yuan Ma, Yuliya Skorobogatko, and Keith Vosseller
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