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| Author | : Ganglong Yang |
| Publisher | : Frontiers Media SA |
| Total Pages | : 231 |
| Release | : 2022-03-14 |
| Genre | : Science |
| ISBN | : 2889746704 |
| Author | : Haojie Lu |
| Publisher | : CRC Press |
| Total Pages | : 258 |
| Release | : 2021-09-21 |
| Genre | : Science |
| ISBN | : 1000406601 |
As one of the most extensive and important protein post-translational modifications, glycosylation plays a vital role in regulating organisms and is associated with various physiological and pathological processes. Recently, researchers have focused on the need to characterize protein glycosylation sites, structures, and their degree of modification, to better understand their biological functions while also looking for potential biomarkers for diagnosis and treatment of disease. Mass spectrometry (MS) is one of the most powerful tools used to study biomolecules including glycoproteins and glycans. With the continuous development of glycoproteomics and glycomics based on MS analysis, more techniques have evolved and contribute to understanding the structure and function of glycoproteins and glycans. This book reviews advancements achieved in MS-based glycoproteomic analysis, including a wide range of analytical methodologies and strategies involved in selective enrichment; as well as qualitative, quantitative, and data analysis, together with their clinical applications. Significant examples are discussed to illustrate the principles, laboratory protocols, and advice for key implementation to ensure successful results. Mass Spectrometry–Based Glycoproteomics and Its Clinic Application will serve as a valuable resource to elucidate new techniques and their applications for students, postdocs, and researchers working in proteomics, glycoscience, analytical chemistry, biochemistry, and clinical medicine. Editor: Haojie Lu is a professor at Fudan University, specializing in proteomics based on mass spectrometry with particular emphasis on novel technologies for separation and identification of low-abundant proteins and post-translationally modified proteins (including glycosylation), as well as relative and absolute quantification methods for proteomics.
| Author | : Haojie Lu |
| Publisher | : CRC Press |
| Total Pages | : 280 |
| Release | : 2021 |
| Genre | : Science |
| ISBN | : 9781003185833 |
As one of the most extensive and important protein post-translational modifications, glycosylation plays very important roles in the organism and is associated with different physiological and pathological processes. Therefore, there has been increasing attention and need to characterize protein glycosylation sites, structures and their modification degree, in order to understand well their biological functions or look for potential biomarkers for disease diagnosis and treatment.Mass spectrometry (MS) is one of the most powerful tools to study biomolecules including glycoproteins and glycans. With the continuous development of glycoproteomics and glycomics based on MS analysis, more and more techniques have appeared and contribute to understanding the structure and function of glycoproteins and glycans. Therefore, this book demonstrates the progress that has been achieved in MS-based glycoproteomic analysis, including a wide range of analytical methodologies and strategies involved in selective enrichment, qualitative analysis, quantitative analysis and data analysis, together with their clinical applications. And some significant examples will be discussed to illustrate the principles, laboratory protocols and key implementation advice to ensure successful results.This book will serve as a valuable resource to appropriate techniques and their applications for students, postdocs, and researchers working in proteomics, glycoscience, analytical chemistry, biochemistry, and clinical medicine, and so on.
| Author | : Elisha Goonatilleke |
| Publisher | : |
| Total Pages | : |
| Release | : 2018 |
| Genre | : |
| ISBN | : 9780438930971 |
Proteins are an important group of biomolecules known to provide a wide range of essential functions. Glycosylation, the enzymatic addition of sugar moieties to the protein, is a commonly occurring post-translational modification and adds greater diversity to the human proteome. Furthermore, protein glycosylation has been known to play key roles in all aspects of human development and health maintenance. Altered glycosylation in a physiological state has a detrimental effect on human health and even initiates many infectious and chronic diseases. However, structural heterogeneity, diversity in individual monosaccharides, and poor ionization efficiencies have made it more challenging to identify and characterize these glycans compared to the other biomolecules. This dissertation presents mass spectrometry-based methods developed to identify, characterize, and quantitate glycosylation in human proteins. Chapter I provides an overview of the structure and function of glycans and glycoproteins, along with key characteristics of mass spectrometry that are required for the analysis of those biomolecules. This includes liquid chromatography-based separation techniques, and mass spectrometry-based ionization and fragmentation methods. Chapter II presents a highly reproducible, sensitive, and rapid method to quantitate proteins and site-specific glycosylation in human milk across lactation using triple quadrupole mass spectrometry. Individual milk proteins including [alpha]-casein, [beta]-casein, [kappa]-casein, [alpha]-lactalbumin, lactoferrin, sectretory immunoglobulin A (SIgA), immunoglobulin M (IgM), immunoglobulin G (IgG) [alpha]-antitrypsin, osteopontin, and lysozyme carried a unique behavior across lactation while changes in site-specific glycosylation had an independent behavior than that of its protein. Chapter III presents a comprehensive comparative glycomic study of immunoglobulin A (IgA) in the milk, saliva, and plasma of individual donors. This study showed N-glycan-specific differences among three body-fluids and observed that the delivery mode can cause changes in IgA N-glycosylation in saliva and plasma IgA while milk IgA remained unchanged. Chapter IV shows a rapid method for the quantification of site-specific glycosylation and site-occupancy in recombinant monoclonal antibody drugs used in cancer therapeutics. Our results revealed that irrespective of the IgG subclass expressed in the drugs, the N-glycopeptide profiles are nearly the same but differ in abundances. Chapter V discusses an in-depth structural analysis of cell surface O-glycans using chip QTOF mass spectrometry.
| Author | : Harald S. Conradt |
| Publisher | : Wiley-Blackwell |
| Total Pages | : 312 |
| Release | : 1991-08-28 |
| Genre | : Science |
| ISBN | : |
Recombinant DNA technology has enabled the efficient production of large quantities of many biologically important glycoproteins by expression in heterologuous mammalian cell lines. In such quantities these glycoproteins can be used not only in basic research but also - after manufacturing by biotechnological means - for commercial purposes. A recent GBF workshop (Braunschweig, Germany, June 1990) was devoted to this highly significant field. In 39 contributions world-leading experts give a state-of-the-art description ranging from basic research reports to perspectives of practical applications. Pharmaceutical companies involved in the production of clinically important glycoproteins (such as immune-modulators, differentiation factors, hormones and receptors) will find this book indispensable. Researchers from industrial laboratories with an emphasis on biotechnology will also find the book invaluable for their daily work.
| Author | : Ajit Varki |
| Publisher | : CSHL Press |
| Total Pages | : 694 |
| Release | : 1999 |
| Genre | : Medical |
| ISBN | : 9780879696818 |
Sugar chains (glycans) are often attached to proteins and lipids and have multiple roles in the organization and function of all organisms. "Essentials of Glycobiology" describes their biogenesis and function and offers a useful gateway to the understanding of glycans.
| Author | : Marija Pezer |
| Publisher | : Springer Nature |
| Total Pages | : 588 |
| Release | : 2021-10-22 |
| Genre | : Medical |
| ISBN | : 3030769127 |
This book summarizes recent advances in antibody glycosylation research. Covering major topics relevant for immunoglobulin glycosylation - analytical methods, biosynthesis and regulation, modulation of effector functions - it provides new perspectives for research and development in the field of therapeutic antibodies, biomarkers, vaccinations, and immunotherapy. Glycans attached to both variable and constant regions of antibodies are known to affect the antibody conformation, stability, and effector functions. Although it focuses on immunoglobulin G (IgG), the most explored antibody in this context, and unravels the natural phenomena resulting from the mixture of IgG glycovariants present in the human body, the book also discusses other classes of human immunoglobulins, as well as immunoglobulins produced in other species and production systems. Further, it reviews the glycoanalytical methods applied to antibodies and addresses a range of less commonly explored topics, such as automatization and bioinformatics aspects of high-throughput antibody glycosylation analysis. Lastly, the book highlights application areas ranging from the ones already benefitting from antibody glycoengineering (such as monoclonal antibody production), to those still in the research stages (such as exploration of antibody glycosylation as a clinical or biological age biomarker), and the potential use of antibody glycosylation in the optimization of vaccine production and immunization protocols. Summarizing the current knowledge on the broad topic of antibody glycosylation and its therapeutic and biomarker potential, this book will appeal to a wide biomedical readership in academia and industry alike. Chapter 4 is available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.
| Author | : Howard J. Allen |
| Publisher | : CRC Press |
| Total Pages | : 704 |
| Release | : 1992-04-15 |
| Genre | : Medical |
| ISBN | : 9780824784317 |
Glycoconjugates Composition: Structure, and Function provides an excellent overview of the composition, biosynthesis, function and structure of the carbohydrate chains of glycoconjugates from higher organisms. It is recommended as a core reference text, providing excellent coverage of the glycoconjugate field.
| Author | : National Research Council |
| Publisher | : National Academies Press |
| Total Pages | : 171 |
| Release | : 2012-10-23 |
| Genre | : Science |
| ISBN | : 0309260868 |
A new focus on glycoscience, a field that explores the structures and functions of sugars, promises great advances in areas as diverse as medicine, energy generation, and materials science, this report finds. Glycans-also known as carbohydrates, saccharides, or simply as sugars-play central roles in many biological processes and have properties useful in an array of applications. However, glycans have received little attention from the research community due to a lack of tools to probe their often complex structures and properties. Transforming Glycoscience: A Roadmap for the Future presents a roadmap for transforming glycoscience from a field dominated by specialists to a widely studied and integrated discipline, which could lead to a more complete understanding of glycans and help solve key challenges in diverse fields.
| Author | : John R. Griffiths |
| Publisher | : John Wiley & Sons |
| Total Pages | : 414 |
| Release | : 2016-11-07 |
| Genre | : Science |
| ISBN | : 1119045851 |
Covers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation Discussion of the chemistry behind each modification, along with key methods and references Contributions from some of the leading researchers in the field A valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post-translational modification research
