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by D. A. Isenberg,T. W. Rademacher

  • ISBN: 0471962600
  • Category: Other
  • Author: D. A. Isenberg,T. W. Rademacher
  • Subcategory: Medicine & Health Sciences
  • Other formats: docx doc txt lrf
  • Language: English
  • Publisher: Wiley; 1 edition (July 1996)
  • Pages: 280 pages
  • FB2 size: 1110 kb
  • EPUB size: 1873 kb
  • Rating: 4.6
  • Votes: 330
Download Abnormalities of IgG Glycosylation and Immunological Disorders fb2

oceedings{itiesOI, title {Abnormalities of IgG glycosylation and immunological . Partial table of contents: The Defining Characteristics of Immunoglobulin Glycosylation (T. Rademacher et a.

Partial table of contents: The Defining Characteristics of Immunoglobulin Glycosylation (T. Analytical Methods 1: Biochemical (P. Williams). Analytical Methods 2: Lectins (N. Sumar). Analytical Methods 3: Monoclonal Antibodies (Y. Wang and G. Rook).

Glycosylation is a major post-translational protein modification and an estimated 2% of the human genome encodes proteins for glycosylation.

17. Nishiura T, Fujii Sh, Kanayama Y, Nishikawa A, Tomiyama Y, Iida M, et al, 1990, Carbohydrate analysis of immunoglobulin G myeloma proteins by lectin and high performance liquid chromatography: role of in the structures. Cancer Res, 50, 5345-50.

They often cause serious, sometimes fatal, malfunction of several different organ systems (especially the nervous system, muscles, and intestines) in affected infants.

Published 1996 by Wiley in Chichester, New York There's no description for this book yet.

Published 1996 by Wiley in Chichester, New York. Includes bibliographical references and index.

Download full-text PDF. Source. To: Maria Monticelli, Tiago Ferro, Jaak Jaeken, Vanessa Dos Reis Ferreira, Paula A Videira.

We also discuss how glycosylation impacts on monoclonal antibodies (mAbs) and IVIg effector functions and how these molecules can be engineered.

These sites consist of asparagine, followed by any amino acid but proline, and either serine or threonine (N-X-S/T).

These sites consist of asparagine, followed by any amino acid but proline, and either serine or threonine (N-X-S/T)

Glycobiology has become the focus of considerable research in recent years as the role of oligosaccharides in both health and disease has come under scrutiny. During this period particular emphasis has been placed on the glycosylation of human immunoglobulins, notably IgG, not least because clear links with a restricted range of human diseases has been established. Abnormalities of IgG Glycosylation and Immunological Disorders uniquely draws together the facts that have emerged to link abnormalities in IgG glycosylation and immunological disease, especially rheumatoid arthritis. It reviews all aspects of immunoglobulin glycosylation abnormalities, including the structural anatomy of glycoproteins; the methods used to analyse them; the clinical aspects of glycobiology in both human disease and animal models; the glycosylation enzymes and the genes that encode and regulate these enzymes; and the possible pathogenicity of IgG. The chapter authors have been chosen because of the original contributions they have made to this exciting field of research. As such this authoritative and well referenced volume will be indispensable to both clinicians and basic scientists with an interest in glycosylation, as well as rheumatologists, immunologists, bacteriologists and glycobiologists.

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