Glycomics : methods and protocols / edited by Nicolle H. Packer, Niclas G. Karlsson.
Contributor(s): Packer, Nicolle | Karlsson, Niclas GMaterial type: TextSeries: Methods in molecular biology (Clifton, N.J.): v. 534.; Springer protocols (Series): Publisher: New York : Humana, ©2009Description: 1 online resource (xiv, 389 pages) : illustrationsContent type: text Media type: computer Carrier type: online resourceISBN: 9781597450225; 1597450227Subject(s): Glycomics | Glycomics | Glycomics | Polysaccharide | Molekularbiologie | Labortechnik | Glykobiologie | Biochemistry | Biology - General | Animal Biochemistry | Chemistry | Biology | Human Anatomy & Physiology | Health & Biological Sciences | Physical Sciences & Mathematics | oligosacchariden | oligosaccharides | glycoproteins | bioinformatics | laboratoriummethoden | laboratory methods | celinteracties | cell interactions | eiwitexpressieanalyse | proteomics | protocollen | protocols | Cellular Biology | CelbiologieGenre/Form: Electronic books. Additional physical formats: Print version:: Glycomics.DDC classification: 572.56 LOC classification: QP601Online resources: Click here to access online
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Includes bibliographical references and index.
Analysis of N- and O-linked glycans from glycoproteins using MALDI-TOF mass spectrometry / Willy Morelle [and others] -- Infrared multiphoton dissociation mass spectrometry for structural elucidation of oligosaccharides / Bensheng Li [and others] -- Mass spectrometry of N-linked glycans / Parastoo Azadi and Christian Heiss -- Solid-phase permethylation for glycomic analysis / Yehia Mechref, Pilsoo Kang, and Milos V. Novotny -- Method for investigation of oligosaccharides using phenylhydrazine derivatization / Erika Lattová and Hélène Perreault -- Two-dimensional HPLC separation with reverse-phase-nano-LC-MS/MS for the characterization of glycan pools after labeling with 2-aminobenzamide / Manfred Wuhrer, Carolien A.M. Koeleman, and André M. Deelder -- Capillary lectin-affinity electrophoresis for glycan analysis / Kazuaki Kakehi and Mitsuhiro Kinoshita -- Analysis of methylated O-glycan alditols by reversed-phase nanoLC coupled CAD-ESI mass spectrometry / Franz-Georg Hanisch and Stefan Müller -- High-throughput and high-sensitivity nano-LC/MS and MS/MS for O-glycan profiling / Hasse Karlsson [and others] -- Collision-induced dissociation tandem mass spectrometry for structural elucidation of glycans / Bensheng Li [and others] -- The structural elucidation of glycosaminoglycans / Vikas Prabhakar, Ishan Capila, and Ram Sasisekharan -- Labelling heparan sulphate saccharides with chromophore fluorescence and mass tags for HPLC and MS separations / Mark Skidmore [and others] -- Small-scale enzymatic digestion of glycoproteins and proteoglycans for analysis of oligosaccharides by LC-MS and FACE gel electrophoresis / Ruby P. Estrella [and others] -- Enrichment strategies for glycopeptides / Shigeyasu Ito, Ko Hayama, and Jun Hirabayashi -- Introductory glycosylation analysis using SDS-PAGE and peptide mass fingerprinting / Nicole Wilson, Raina Simpson, and Catherine Cooper-Liddell -- Characterization of N-linked glycosylation on recombinant glycoproteins produced in Pichia pastoris using ESI-MS and MALDI-TOF / Bing Gong [and others] -- N-glycosylation site analysis of human platelet proteins by hydrazide affinity capturing and LC-MS/MS / Urs Lewandrowski and Albert Sickmann -- LC/MSn for glycoprotein analysis : N-linked glycosylation analysis and peptide sequencing of glycopeptides / Nana Kawasaki, Satsuki Itoh, and Teruhide Yamaguchi -- Detecting the "O-GlcNAcome" : detection, purification, and analysis of O-GlcNAc modified proteins / Natasha E. Zachara -- Preparation of a glycan library using a variety of glycosyltrasferases [i.e. glycosyltransferases] / Hiromi Ito [and others] -- Data mining the PDB for glyco-related data / Thomas Lütteke and Claus-W. von der Lieth -- Saccharide microarrays for high-throughput interrogation of glycan-protein binding interactions / Andrew K. Powell, Zheng-liang Zhi, and Jeremy E. Turnbull -- Glycosaminoglycan characterization methodologies probing biomolecular interactions / Vikas Prabhakar, Ishan Capila, and Ram Sasisekharan -- Development and characterization of antibodies to carbohydrate antigens / Jamie Heimburg-Molinaro and Kate Rittenhouse-Olson -- Inhibition of glycosyltransferase activities as the basis for drug development / John Schutzbach and Inka Brockhausen -- Saturation transfer difference NMR spectroscopy as a technique to investigate protein-carbohydrate interactions in solution / Thomas Haselhorst, Anne-Christin Lamerz, and Mark von Izstein.
Print version record.
Due to the significant contributions of carbohydrates to the functional diversity of the cell, the challenging study of the glycome has expanded beyond the research of carbohydrate experts and into the wider scope of the life sciences. To aid all scientists now delving into this vital subject area, Glycomics: Methods and Protocols collects a compendium of detailed laboratory protocols reflecting the increasing availability of sample preparation, chromatographic, electrophoretic, mass spectrometric, and bioinformatic tools specifically designed for the analysis of glycosylation. Leading researchers in the field address subjects such as glycoprotein and proteoglycan analysis, glycosylation structure determination, as well as various approaches to investigate the interaction between glycans and a variety of carbohydrate-recognizing proteins in order to aid exploration into the functional significance of the oligosaccharides. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Glycomics: Methods and Protocols serves as a valuable guide for experimenters facing the challenges of glycan analysis in hope of providing further insights into the biology of cell-cell communication and interaction.