The Antibody Molecule reviews the literature leading to current knowledge of the structure of immunoglobulins. The book begins by outlining some of the basic structural characteristics of immunoglobulins without citing the references on which the information is based. Separate chapters follow covering the chemical nature of the active site of an antibody molecule and mechanisms of interaction with hapten; the general structural features and properties of the various classes of human immunoglobulin; and amino acid sequences of human and mouse L chains and of human and rabbit H chains. Subsequent chapters deal with the evolution of the immunoglobulin classes; special properties of mouse, guinea pig, rabbit, and horse immunoglobulins; idiotypic specificities of immunglobulins; and the genetic control of antibodies.
This book is meant for immunologists who have not personally observed the development of this exciting period in the history of immunology. It will also provide useful supplemental reading for the serious student or investigator who wishes to become familiar with the nature of the antibody molecule, its genetic control, and mode of action.

Contenu

Preface
1 General Structural Features of Immunoglobulin Molecules; Myeloma Proteins
Myeloma and Bence Jones Proteins
Nomenclature
References
2 Nature of the Active Site of an Antibody Molecule and the Mechanism of Antibody-Hapten Interactions
I. Inhibition of Precipitation by Haptens and Chemical Modification as Probes for Antibody Specificity
II. Specificity of Antibodies to Synthetic Polypeptides
III. Stabilization of the Antibody Molecule by Interaction with Hapten
IV. Induction of Optical Activity in Hapten Bound to Antibody
V. The Question of Conformational Changes Induced in Antibodies upon Interaction with Antigen or Hapten
VI. Rates and Energetic Aspects of Antigen-Antibody Reactions
VII. Affinity Labeling of Antibody Molecules or Myeloma Proteins with Antibody Activity
References
3 Human Immunoglobulins
I. General Structural Properties
II. Kappa and Lambda Chains
III. IgG and Its Subclasses
IV. Structure and Properties of Human IgM
V. Structure and Properties of Human IgA
VI. IgE
VII. IgD
VIII. Microglobulin ()
IX. Rheumatoid Factors
References
4 Amino Acid Sequences in Human Immunoglobulins and in Mouse Light Chains
I. Introduction
II. Numbering System
III. Amino Acid Sequences in Human L Chains
IV. Amino Acid Sequences in L Chains of the Mouse
V. Common Evolutionary Origin of K and A Chains of Human and Mouse Origin
VI. Amino Acid Sequences in Rabbit K Chains
VII. Amino Acid Sequences in Human and Rabbit H Chains
VIII. Amino Acid Sequence of Microglobulin
IX. Amyloidosis
X. Carbohydrate in Immunoglobulins
References
5 The Three-Dimensional Structure of Immunoglobulins
I. X-Ray Crystallography
II. Physicochemical Investigations Relating to Three-Dimensional Structure
References
6 Properties and Interactions of the Light and Heavy Chains of Immunoglobulins
I. Introduction
II. Separation of Light and Heavy Chains
III. Solubility and Conformational Properties of the Isolated Chains
IV. Antibody Activity in Isolated Chains and in Recombinants of Heavy and Light Chains
V. Interaction of VL or CL Segments of Light Chains with Intact Heavy Chains
VI. Stability of Fragments Consisting Only of V Domains
VII. Effect of Hapten on the Strength of Interaction of H and L Chains
VIII. Contribution to Antibody Activity of Isolated H and L Chains
IX. Half-Molecules of IgG
References
7 Evolution of the Immunoglobulins
I. Introduction
II. Universality of IgM-Like Molecules in Vertebrates
III. Immunoglobulins of Fish
IV. Immunoglobulins of Amphibia
V. Immunoglobulins of Reptiles
VI. Immunoglobulins of Birds; Appearance of IgA
VII. Carbohydrate Content of Immunoglobulins from Various Species on the Phylogenetic Scale
VIII. Phylogeny of IgA, IgE, IgG Subclasses, Light Chain Types, and the VHm Subgroup
IX. Selective Advantages in the Evolution of Immunoglobulin Classes
References
8 Immunoglobulins of the Rabbit, Mouse, Guinea Pig, and Horse
I. Introduction
II. General Considerations
III. Antigeiiic Relationships
IV. Homocy to tropic Antibodies: IgE
V. Rabbit Immunoglobulins
VI. Guinea Pig Immunoglobulins
VII. Mouse Immunoglobulins
VIII. Horse Immunoglobulins
IX. Passive Cutaneous Anaphylactic Reactions in Guinea Pigs Mediated by Heterologous Immunoglobulins
References
9 Allotypes of Rabbit, Human, and Mouse Immunoglobulins
I. Introduction
II. Rabbit Allotypes
III. Human Allotypes
IV. Mouse Allotypes
V. Suppression of Allotypic Specificities
References
10 Homogeneous Antibodies and Myeloma Proteins with Antibody Activity
I. Introduction
II. Homogeneous Antistreptococcal Antibodies
III. Homogeneous Antibodies to Pneumococcal Polysaccharides
IV. Homogeneous Antihapten Antibodies
V. Relationship of Structure of Antigen to the Degree of Heterogeneity of Antibody
VI. Restricted Heterogeneity of Human Antibodies to Polysaccharide Antigens
VII. Influence of Genetic Factors on the Magnitude of the Response of Rabbits to Streptococcal Antigens
VIII. Influence of Genetic Factors on the Heterogeneity of Rabbit Antibodies Produced against Streptococcal Antigens
IX. Amino Acid Sequences of Homogeneous Rabbit Antibodies
X. Cold Agglutinins from Patients with Chronic Cold Hemagglutinin Syndrome (CHS)
XI. Rheumatoid Factors and Cryoglobulins
XII. Human Monoclonal Proteins with Antibody Activity toward Antigens Other than IgG
XIII. Mouse Myeloma Proteins with Antibody Activity
XIV. Summary of Evidence Relating Myeloma Proteins with Specific Binding Activity to Induced Antibodies
XV. Unusual Immunological Cross-Reactions
XVI. Antibody Activity in Crystallized Fab' Fragments
XVII. Induction of Homogeneous Antibody after Adoptive Transfer of Limited Numbers of Cells
References
11 Idiotypic Specificities of Immunoglobulins
I. Introduction
II. Idiotypic Specificities in Human Monoclonal Proteins
III. Idiotypic Specificities in Rabbit and Human Antibody Populations
IV. Idiotypic Cross-Reactions among Rabbit Antibodies
V. Idiotypic Cross-Reactions among Antibodies and Myeloma Proteins of Inbred Mice
VI. Evidence Based on Idiotypic Specificity for Limited Heterogeneity of Normal Antibody Populations
VII. Persistence and Changes of Antibody Populations during Prolonged Immunization
VIII. Shared Idiotypic Determinants in Rabbit Antibodies or Human Myeloma Proteins Belonging to Different Classes
IX. Localization of Idiotypic Determinants
X. Cross-Reactions of Antudiotypic Antibodies with Nonspecific Immunoglobulins
XI. Suppression of Idiotypic Specificities
XII. Production of Antudiotypic Antibodies within the Same Strain of Mouse; Antitumor Activity of Antimyeloma Protein Antibodies
XIII. Production of Antudiotypic Antibodies by an Animal against Its Own Antibodies
References
12 Theories of the Genetic Control of Diversity of Antibodies
I. Introduction
II. RNA-DNA Hybridization
III. Basic Premises Relevant to Theories of Antibody Diversity
IV. Theories of Antibody Diversity
V. Strengths and Weaknesses of the Various Theories
VI. Repeated Occurrence of Monoclonal Proteins with Identical
V Regions
References
Index