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1. |
Record Nr. |
UNINA9910506382203321 |
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Titolo |
Antibody glycosylation / / edited by Marija Pezer |
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Pubbl/distr/stampa |
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Cham, Switzerland : , : Springer, , [2021] |
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©2021 |
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ISBN |
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Descrizione fisica |
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1 online resource (585 pages) |
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Collana |
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Experientia Supplementum Ser ; ; v.112 |
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Disciplina |
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Soggetti |
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Biochemical markers |
Pharmacology |
Immunology |
Enginyeria de proteïnes |
Enginyeria bioquímica |
Llibres electrònics |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Nota di bibliografia |
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Includes bibliographical references and index. |
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Nota di contenuto |
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Intro -- Foreword -- Contents -- Editor and Contributors -- Chapter 1: Micro-Heterogeneity of Antibody Molecules -- 1.1 Introduction -- 1.2 Disulfide Bond-Related Modifications -- 1.3 N- and C-Terminal Modifications -- 1.3.1 N-Terminal Modifications -- 1.3.2 C-Terminal Modifications -- 1.4 Chemical Modifications of Main-Chain Amino Acid Residues -- 1.4.1 Deamidation -- 1.4.2 Glycation -- 1.4.3 Oxidation -- 1.5 Aggregation -- 1.6 Glycosylation -- 1.6.1 IgG-Fc Oligosaccharide Chain -- 1.6.2 Fab Oligosaccharide Chain -- 1.7 Conclusion -- References -- Part I: Analytical Methods -- Chapter 2: Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 2.1 Introduction -- 2.1.1 Glycosylation -- 2.1.2 Immunoglobulins -- 2.2 Liquid Chromatography -- 2.2.1 Immunoglobulin Purification by Liquid Chromatography -- 2.2.1.1 Affinity Chromatography -- 2.2.1.2 Melon Gel Chromatography -- 2.2.1.3 Size-Exclusion Chromatography (SEC) -- 2.2.1.4 Ion-Exchange Chromatography (IEX) -- 2.2.2 N-Glycan Analysis by Liquid Chromatography -- 2.2.2.1 Glycan Release -- 2.2.2.2 Fluorescent Labeling Methods -- 2.2.2.3 Reducing Agent -- 2.2.2.4 Clean-Up |
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Strategies -- 2.2.2.5 Detection of Labeled Glycans with (U)HPLC -- 2.2.2.6 N-Glycan Sequencing by Exoglycosidases -- 2.2.3 O-Glycan Analysis by Liquid Chromatography -- 2.2.4 Liquid Chromatography Coupled to Mass Spectrometry -- 2.2.4.1 Proteolytic Cleavage -- 2.2.4.2 Glycopeptide and Glycan Enrichment -- 2.2.4.3 Glycopeptide and Glycan Analysis by LC-MS -- 2.2.4.4 Analysis of Ig Glycosylation on the Subunit and Whole Protein Level -- 2.3 Lectin Techniques -- 2.3.1 Lectin Chromatography -- 2.3.2 Lectin Microarrays -- 2.4 Perspectives -- References -- Chapter 3: Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis -- 3.1 Basic Principles of Mass Spectrometry. |
3.1.1 Ionization -- 3.1.2 Gas-Phase Separation and Detection -- 3.1.3 Tandem MS -- 3.2 Levels of IgG N-Glycosylation Analysis -- 3.3 Sample Preparation for IgG Glycosylation Analysis -- 3.3.1 Protein A, G, and L Affinity Chromatography for IgG Enrichment from Biological Samples -- 3.3.1.1 Protein A -- 3.3.1.2 Protein G -- 3.3.1.3 Protein L -- 3.3.1.4 Recombinant Fusion Proteins and Alternative Scaffolds -- 3.3.2 Sample Preparation for Released IgG Glycan Analysis -- 3.3.2.1 Chemical and Enzymatic Glycan Release -- 3.3.3 Fluorescent and Isotopic Glycan Labeling -- 3.3.4 Sample Preparation for Glycopeptide Mapping and Subclass-Specific IgG Fc Glycosylation Analysis -- 3.3.4.1 Enzymatic Digestion -- 3.3.4.2 Stable Isotope Glycopeptide Labeling -- 3.3.4.3 Glycan and Glycopeptide Enrichment and Purification Strategies -- 3.4 Deciphering the IgG Glycan Structure -- 3.4.1 Fragmentation -- 3.4.2 Fragmentation Nomenclature -- 3.4.3 Fragmentation Candidates -- 3.4.3.1 Fragmentation of Glycopeptides -- 3.4.3.2 Fragmentation of Released Glycans -- 3.4.4 Ionization Polarity of MS Analysis -- 3.4.4.1 Example of Positive Ion Mode Fragmentation -- 3.4.4.2 Example of Negative Ion Mode Fragmentation -- 3.4.5 Exoglycosidase Digestion Monitored by MS -- 3.5 Selected Approaches for IgG Glycosylation Analysis -- 3.5.1 MALDI-MS -- 3.5.1.1 Intact Proteins and Glycopeptides -- 3.5.1.2 Released N-Glycans -- 3.5.1.3 Sialic Acid Stability -- 3.5.1.4 Matrix Substances for MALDI-MS -- 3.5.1.5 MALDI-MS for High-Throughput and Quantitative Analysis -- 3.5.2 LC-MS for IgG Glycosylation Analysis -- 3.5.2.1 Coupling LC to MS for Enhanced Separation and Structural Characterization -- 3.5.2.2 HILIC-UHPLC-MS -- 3.5.2.3 RP-LC-MS -- 3.5.2.4 PGC for Enhanced Isomeric Glycan Separation -- 3.5.2.5 Anion Exchange LC-MS -- 3.5.2.6 Challenges of Miniaturization. |
3.5.3 Capillary Electrophoresis-Mass Spectrometry -- 3.6 Perspectives -- References -- Chapter 4: Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 4.1 Historical Background -- 4.2 Background: Principles of Capillary (Gel) Electrophoresis (C(G)E) -- 4.3 Performance, Benefits, and Potentials of Capillary (Gel) Electrophoresis C(G)E -- 4.4 Data Analysis and Interpretation -- 4.5 Exoglycosidase Sequencing of Glycans -- 4.6 Coupling Capillary Electrophoresis with Mass Spectrometry -- 4.7 Latest Developments: Miniaturization of CE Systems-Microchip CE -- 4.8 Application of C(G)E for Immunoglobulin Analysis -- 4.9 Conclusion -- References -- Chapter 5: Automation of Immunoglobulin Glycosylation Analysis -- 5.1 Introduction -- 5.1.1 Biopharmaceutical Glycomics -- 5.1.2 Clinical Glycomics -- 5.1.3 Towards High-Throughput Glycomics -- 5.1.4 Robotics: The Ultimate High-Throughput Solution? -- 5.2 Automation of Glycomics Sample Preparation -- 5.2.1 Sample Origins and Protein Purification -- 5.2.1.1 Serum and Plasma -- 5.2.1.2 Therapeutic Antibody Glycoproteins -- 5.2.2 Preparing Glycans for Analysis: Glycan Release, Derivatization and Clean-Up -- 5.2.2.1 Plasma and Serum -- Automated Methods for N- |
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Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.2.2 Therapeutic Antibody Glycoproteins -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.3 Automated Methods for Glycopeptide Preparation -- 5.3 Commentary -- 5.4 Future Perspectives -- 5.5 Conclusions -- References -- Chapter 6: Bioinformatics in Immunoglobulin Glycosylation Analysis -- 6.1 Introduction. |
6.2 Glycomic Data Collection and Processing -- 6.2.1 Reference Databases -- 6.2.2 Identification and Quantification Software Tools -- 6.3 Glycoproteomics Data Collection and Processing -- 6.3.1 Reference Databases -- 6.3.2 Identification Software Tools -- 6.3.3 Quantification Software Tools -- 6.4 Data Integration with Other Omics -- 6.5 Practical Examples -- 6.5.1 Glycomic Data Processing -- 6.5.1.1 Software Required -- 6.5.1.2 Glycan Composition Determination -- 6.5.1.3 Annotation of MS and MS/MS Glycomics Spectra -- 6.5.1.4 Convert Raw Mass Spectrometry Data to mzXML -- 6.5.1.5 Skyline for Glycomics Quantitation -- 6.5.1.6 Setting Up Transition List -- 6.5.2 Glycopeptide Data Processing for Enriched Immunoglobulins -- 6.5.2.1 Software Required -- 6.5.2.2 Glycosylation Site Identification Based on MS2 -- 6.5.2.3 Glycoform Identification Based on MS1 -- 6.5.2.4 Targeted Glycopeptide Quantification -- 6.5.3 Visualizing Profiles -- 6.5.3.1 Structural Dependencies Brought Out by GlyConnect Compozitor -- 6.5.3.2 Comparing Profiles with Glynsight -- 6.6 Conclusion -- References -- Part II: Biosynthesis and Regulation -- Chapter 7: N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome -- 7.1 Introduction -- 7.2 Biosynthesis of N-Glycans in the Endoplasmic Reticulum -- 7.2.1 Building Blocks for N-Glycan Synthesis -- 7.2.2 Precursor Synthesis and Its Attachment to Nascent Polypeptide Chains -- 7.2.3 N-Glycan Processing in the ER and Quality Control -- 7.3 N-Glycan Processing in the Golgi Apparatus -- 7.3.1 N-Glycosylation of Immunoglobulins -- 7.4 Golgi Microenvironment Is Important for Normal Processing and Maturation of N-Glycans -- 7.4.1 Golgi pH Homeostasis -- 7.4.2 Golgi Ion Homeostasis -- 7.4.3 Golgi Redox State -- 7.5 Concluding Remarks -- References -- Chapter 8: Genetic Regulation of Immunoglobulin G Glycosylation. |
8.1 Introduction -- 8.2 Heritability of the Human IgG N-Glycome -- 8.3 Linkage Studies of Mouse N-glycome -- 8.4 Genome-Wide Association Studies of Human N-Glycome -- 8.4.1 Genomic Loci Associated with IgG N-Glycosylation -- 8.4.1.1 Chromosome 1 -- 8.4.1.2 Chromosome 3 -- 8.4.1.3 Chromosome 5 -- 8.4.1.4 Chromosome 6 -- 8.4.1.5 Chromosome 7 -- 8.4.1.6 Chromosome 9 -- 8.4.1.7 Chromosome 11 -- 8.4.1.8 Chromosome 14 -- 8.4.1.9 Chromosome 17 -- 8.4.1.10 Chromosome 21 -- 8.4.1.11 Chromosome 22 -- 8.4.2 Suggestive Associations -- 8.4.3 Functional Network of Loci Associated with IgG Glycosylation -- 8.5 Pleiotropy with Complex Traits and Diseases -- 8.6 Conclusions -- References -- Chapter 9: Epigenetics of Immunoglobulin G Glycosylation -- 9.1 Introduction -- 9.2 Regulation of Glycosyltransferases by Transcription Factors -- 9.3 Epigenetic Regulation of IgG Glycosylation -- 9.4 The Role of miRNAs in Protein N-Glycosylation -- 9.5 Conclusions -- References -- Chapter 10: Immunoglobulin G Glycosylation Changes in Aging and Other Inflammatory Conditions -- 10.1 Premise -- 10.2 IgG Glycosylation -- 10.3 Changes in IgG Asn297 Glycans Associated with Inflammatory Diseases -- 10.4 IgG Glycosylation as a Predictor of Disease Onset, |
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Progression, and Therapy Response -- 10.4.1 Prediction of Disease Onset -- 10.4.2 Prediction of Progression and Therapy Response -- 10.5 IgG Glycosylation in Aging -- 10.6 The Inflammaging Is a Link Between Aging and Inflammation -- 10.7 How Altered IgG Glycosylation Drives Inflammation -- 10.7.1 Activation of Complement Through the Lectin or the Classical Pathways -- 10.7.2 Binding to Fcγ Receptors -- 10.7.3 Binding on Lectin Receptors of Antigen-Presenting Cells: Role in the Intravenous Administration of High Doses IgG (IVIG) -- 10.7.4 Anti IgG Autoantibodies -- 10.8 Molecular Bases of N-Glycosylation Changes -- 10.9 Conclusions. |
References. |
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2. |
Record Nr. |
UNINA9910695723203321 |
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Autore |
Allen Tim (John Timothy), <1953-> |
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Titolo |
Information resources on induced molting in chickens, 1902-2002 [[electronic resource] /] / Tim Allen |
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Pubbl/distr/stampa |
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Beltsville, MD : , : U.S. Dept. of Agriculture, Agricultural Research Service, National Agricultural Library, Animal Welfare Information Center, , [2002] |
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Descrizione fisica |
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1 electronic text : digital, HTML file |
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Collana |
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AWIC resource series ; ; no. 14 |
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Soggetti |
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Molting |
Hens |
Animal welfare |
Hens - Nutrition |
Eggs - Production |
Veterinary drugs |
Physiology |
Bibliographies. |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based on content viewed Oct. 26, 2002; title from web page. |
"September 2002." |
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Sommario/riassunto |
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This publication is a comprehensive bibliography documenting US Department of Agriculture funded research into various aspects of induced molting in laying hens and world literature on induced molting of laying hens. Topics covered include salmonella, poultry welfare, management strategies for inducing a molt, economics of molting, and physiological consequences of induced molting. Numerous websites with full-text animal welfare guidelines from industry, scientific articles from poultry researchers, and position papers from professional societies are included. |
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3. |
Record Nr. |
UNINA9910819379403321 |
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Autore |
Rapetti Thalie |
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Titolo |
La politique, peut-on la quitter vraiment ? / / Thalie Rapetti |
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Pubbl/distr/stampa |
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Clichy : , : Éditions Marie B, , [2018] |
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©2018 |
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ISBN |
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Descrizione fisica |
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1 online resource (223 pages) |
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Disciplina |
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Soggetti |
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Cabinet officers - France |
Politics, Practical - France - History - 20th century |
Politics, Practical - France - History - 21st century |
France Politics and government 1958- |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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