The Immunoglobulins: Structure and Function

The Immunoglobulins: Structure and Function

by Roald Nezlin
The Immunoglobulins: Structure and Function

The Immunoglobulins: Structure and Function

by Roald Nezlin

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Overview

This book provides comprehensive up-to-date information on the structure and function of immunoglobulins. It describes the basic features of these molecules, which assists the reader in understanding how they function as an integral part of the immune system. The Immunoglobulins describes the localization and structure of different binding sites of immunoglobulin molecules, including the antigen-binding site, on the basis of latest x-ray crystallography studies. It discusses recently developed biotechnological methods that allow scientists to obtain fully active antibody molecules in vitro even without immunization and to construct new variants of immunoglobulins and their fragments by fusing with various other active molecules. A survey of recent knowledge on immunoglobulin-binding molecules other than antigens and on flexibility of immunoglobulin molecules concludes the discussion of functional aspects of the problem.
  • Describes recent reviews on the structure and function of immunoglobulin molecules of various species
  • Summarizes in detail recent findings on the fine structure of the antigen-combining site
  • Presents comparative data on the antigen-recognizing sites of other molecules such as MHC proteins and T-cell receptors
  • Summarizes growing data on immunoglobulin binding sites responsible for the reaction of immunoglobulins with molecules other than antigens
  • Explores the rapid advance of recent biotechnological methods used for the construction of antibody molecules and their fragments with new properties
  • Presents extensive references and is lavishly illustrated

Product Details

ISBN-13: 9780080534527
Publisher: Elsevier Science
Publication date: 05/06/1998
Sold by: Barnes & Noble
Format: eBook
Pages: 269
File size: 9 MB

Table of Contents

Preface.Structural Aspects:General Characteristics of Immunoglobulin Molecules: Immunoglobulin Classes.Heterogeneity of Immunoglobulins.Detection and Isolation of Immunoglobulins.Proteolytic and Chemical Fragments of Immunoglobulins.Immunoglobulin Peptide Chains.Additional Peptide Chains.Immunoglobulin Fold (Domain).Fab Portion.Fc Portion.Immunoglobulin Molecules.Carbohydrate Components of Immunoglobulins.Animal and Human Immunoglobulins:Low Vertebrates.Birds.Mammals.Human Immunoglobulins.Origin of Antibody Diversity in Mice and Humans.Evolutionary Aspects.Engineering Antibody Molecules:Problems of Serum Immunotherapy.Chimeric Antibody Molecules and Humanization.Minimal Antibody Fragment (Fv).Production of Human Monoclonal Antibodies by Page-Display and Transgene Technologies.Engineering of Immunoglobulins with Novel Properties.Polymerization of IgG Molecules and Their Fragments.Bispecific Antibodies.Functional Aspects:Antigen-Combining Site:General Characteristics.Conformational Changes Linked with Antigen Binding.Complex of VH of Camelid Heavy Chain Antibodies with Antigen.Interaction of an Autoantibody (Rheumatoid Factor) with Fcg.Structural Aspects of Antibody Specificity.Modeling Antibody-Combining Sites.Structural Aspects of Catalytic Antibody Activity. Antigen-Recognizing Molecules Other Than Antibodies:T-Cell Antigen Receptor.Proteins of Major Histocompatibility Complex.Complexes of T-Cell Receptor and Peptide-MHC.CD1 Molecules.Natural Killer Cell Inhibitory Receptors.Comparison of Antigen Binding by Various Antigen-Recognizing Molecules.Interactions Outside the Antigen-Combining Site:Fc Receptor-Binding Sites.Complement-Binding Sites.Proteins Reacting with the Fc Portion.Proteins Reacting with the Fab Portion.Lectins.Molecular Chaperones.Bacterial Immunoglobulin-Binding Proteins.Segmental Movements of Immunoglobulin Molecules:General Aspects.Functional Aspects of Segmental Flexibility.Subject Index.

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Awarded the Highest Rating by Doody's Publishing Reviews — 5 Stars!Selected as one of the 250 Best Books of 1998 by DOODY'S JOURNAL!

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