Research Catalog

Title

Recombinant antibodies / [edited by] Frank Breitling, Stefan Dübel.

Publication

New York : John Wiley, [1999], ©1999.

Items in the Library & Off-site

Holdings

Details

Additional Authors

• Dübel, Stefan.
• Breitling, Frank.

Description

viii, 161 pages : illustrations; 26 cm

Subjects

• Antibodies
• Recombinant Proteins
• Antibody Formation
• Recombinant antibodies

Bibliography (note)

• Includes bibliographical references (p. 146-154) and index.

Contents

• Ch. 1. Background. 1.1. How the Body Manufactures Antibodies. 1.1.1. The Chance Combination of Peptide Building Blocks Leads to a Vast Variety of Antibodies. 1.1.2. The Specificity of Antigen Binding is Determined by the Hypervariable Domains. 1.1.3. The Constant Regions Stabilize the Antibody Molecule. 1.1.4. The Constant Regions Mediate the Effector Functions. 1.1.5. Antibody Binding Improves During an Immune Response. 1.1.6. B-Lymphocytes are Expanded through Clonal Selection. 1.1.7. Only those Memory Cells Survive that Code for Higher Affinity Antibodies. 1.1.8. Evolution Invented Antibody Engineering Millions of Years Ago. 1.2. Antibody Production: Established Methods and New Approaches. 1.2.1. Antibodies are Widely Used in Research and Diagnosis. 1.2.2. Antisera Contain Polyclonal Antibodies. 1.2.3. Immortal B-Lymphocytes Produce Monoclonal Antibodies. 1.2.4. Recombinant Antibodies are Genetically Engineered Antibody Fragments.
• 1.2.5. Fv Fragments are the Smallest Antigen-Binding units. 1.2.6. Why Recombinant Antibodies? -- Ch. 2. Building Recombinant Antibody Fragments. 2.1. Introduction. 2.1.1. Bacteria can Produce Recombinant Antibody Fragments. 2.1.2. The Humoral Immune System can be Imitated in Bacteria. 2.2. Sources of Antibody Genes. 2.2.1. Combinatorial Assembly of Antibody Genes. 2.2.2. Complexity of Antibody Gene Libraries. 2.2.3. What is the real Complexity of Antibody Gene Libraries? 2.2.4. Cloning Antibody Genes from Hybridoma Cell Lines. 2.2.5. Gene Libraries from Immunized Donors. 2.2.6. Universal Antibody Gene Libraries from Nonimmunized Donors. 2.2.7. Genomic Antibody Gene Libraries. 2.2.8. Hybrid and Semisynthetic Antibody Gene Libraries. 2.2.9. Synthetic Antibody Gene Libraries with Random Sequences in the CDRs. 2.2.10. In Vivo Recombination Systems enable "Superlibraries" 2.3. From Diversity to Specifity: The Selection of Recombinant Antibodies from Gene Libraries.
• 2.3.1. Selection of Recombinant Antibodies with Classical Expression Systems. 2.3.2. Genes Coupled to their Gene Products. 2.3.3. Peptides can be Presented on the Surface of Bacteriophages. 2.3.4. Recombinant Antibodies Anchored on the Surface of Filamentous Phages. 2.3.5. Billions of Different Antibody Clones can be Tested for Binding with the Help of Display Vectors. 2.3.6. Display Vectors Simplify the Selection of Human Recombinant Antibody Fragments. 2.3.7. Antigen-Specific Infection of Bacteria. 2.3.8. Other Prokaryotic Display Vectors. 2.3.9. Antibodies can also be Anchored on the Surface of Eukaryotic Viruses. 2.4. Antibody Engineering. 2.4.1. Why Antibody Engineering? 2.4.2. Mouse-Human Chimeras. 2.4.3. Framework Regions of the Variable Domain from Mouse Antibodies can be Humanized. 2.4.4. Three-Dimensional Structure of Antibodies can be Modeled on a Computer. 2.4.5. Efficient Screening Systems help in the Humanization of Antibodies through Chain Shuffling.
• 2.4.6. Affinity of Recombinant Antibodies can be Increased by Repeated Mutation and Selection. 2.4.7. Antibody Genes can be Mutated with Gene Synthesis or with the Help of the Polymerase Chain Reaction. 2.4.8. "Sexual" PCR Combines Several Mutations. 2.4.9. Fv Fragments are Stabilized through a Peptide Bond Linking the Variable Domains. 2.4.10. Fv Fragments can be Stabilized through Internal Disulfide Bridges. 2.4.11. Camel Antibodies Contain only One Variable Domain. 2.4.12. Antibodies can take over the Function of Enzymes. 2.5. Summary -- Ch. 3. Antibodies With New Functions. 3.1. Why Bispecific and Bifunctional Antibodies? 3.2. New Functions through Homologous Fusion Partners: Bispecific Antibodies. 3.2.1. Bispecific Antibodies Unite the Binding Properties of Two Different Monoclonal Antibodies into One Molecule. 3.2.2. Recombinant Production of Bispecific Antibodies. 3.2.3. Creating Bispecific Antibodies with Help from Heterologous Binding Domains.
• 3.2.4. "Universal" Bispecific Antibodies. 3.2.5. Recombinant Bispecific Antibodies can be Distinctly Smaller than an IgG. 3.3. New Functions through Heterologous Fusion Partners: Bifunctional Antibodies. 3.3.1. What are Bifunctional Antibodies? 3.3.2. Bifunctional Antibodies can be Used as Immunotoxins. 3.3.3. Radioimmunotoxins. 3.3.4. Intracellular Antibodies. 3.3.5. Recombinant Antibodies can be Anchored on the Surface of Cells. 3.4. Summary -- Ch. 4. Production and Purification of Recombinant Antibody Fragments. 4.1. Properties of Recombinant Antibodies and Choice of Expression System. 4.1.1. Structural Characterization of an Antibody: The Definition of the Hypervariable Regions (CDRs).

ISBN

0471178470

LCCN

99014610

OCLC

ocm40964704

Owning Institutions

Columbia University Libraries