Immunoglobulins

1. Front Matter

   Pages i-xvii

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2. Studies on the Three-Dimensional Structure of Immunoglobulins

   • Roberto J. Poljak

   Pages 1-36

3. Solution Conformation and Segmental Flexibility of Immunoglobulins

   • Renata E. Cathou

   Pages 37-83

4. The Affinity of Antibody: Range, Variability, and the Role of Multivalence

   • Fred Karush

   Pages 85-116

5. Antibody Combining Regions

   • Frank F. Richards, Robert W. Rosenstein, Janos M. Varga, William H. Konigsberg

   Pages 117-154

6. The Secretory Component and the J Chain

   • Charlotte Cunningham-Rundles

   Pages 155-172

7. The Structural Basis for the Biological Properties of Immunoglobulins

   • J. Michael Kehoe

   Pages 173-196

8. The Significance of Gene Duplication in Immunoglobulin Evolution (Epimethean Natural Selection and Promethean Evolution)

   • Susumu Ohno

   Pages 197-204

9. The Phylogenetic Origins of Immunoglobulin Structure

   • Gary W. Litman, J. Michael Kehoe

   Pages 205-228

10. Evidence for and the Significance of ‘Two Genes, One Polypeptide Chain’

    • An-Chuan Wang

    Pages 229-255

11. Structure of Atypical Immunoglobulins—Relationship to Genetic Control Mechanisms

    • Blas Frangione

    Pages 257-272

12. Patterns of Sequence Variability in Immunoglobulin Variable Regions: Functional, Evolutionary, and Genetic Implications

    • J. Michael Kehoe, J. Donald Capra

    Pages 273-295

13. Genetic Control of Immunoglobulin Synthesis in Man

    • Andreas Morell, Silvio Barandun

    Pages 297-310

14. Heavy-Chain Variable (VH) Subgroups among Myeloma Proteins, Antibodies, and Membrane Immunoglobulins of Lymphocytes

    • J. B. Natvig, Ø. Førre, T. E. Michaelsen

    Pages 311-321

15. Cryoglobulins and Pyroglobulins

    • Horace H. Zinneman

    Pages 323-343

16. Biosynthesis and Secretion of Immunoglobulins

    • Yong Sung Choi

    Pages 345-355

17. Lymphocyte Membrane Immunoglobulins: An Overview

    • Benvenuto Pernis

    Pages 357-372

18. Back Matter

    Pages 373-381

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Since the discovery more than thirty years ago that antibody actlvlty could be localized to discrete plasma protein fractions, the study of immunoglobulin struc­ ture and function has dominated the field of immunochemistry. During this time, sources of homogeneous immunoglobulin molecules have been discovered, the subunit nature of the proteins has been defined, and the three-dimensional struc­ tures of the antigen-recognition portion of several antibody molecules have been elucidated. Insights into the complicated genetic control of these proteins are being gained rapidly through analysis of amino acid sequences of naturally occurring and induced homogeneous immunoglobulins. Immunoglobulins have been analyzed by protein chemists as models of complex multimeric systems, examined by geneticists studying serum protein polymorphisms, and employed by molecular biologists as highly selective probes capable of distinguishing minor features of molecular topog­ raphy. Clinical applications have ranged from the now routine quantitation of immunoglobulin levels to the use of antibodies to detect trace levels of a variety of natural products and drug metabolites. All these applications have depended ulti­ mately on a thorough understanding of the immunoglobulin and its antigen-combin­ ing site. To cover the entire field of immunoglobulin structure and function would require many volumes this size; therefore, subjects presented in this volume represent those which we felt contribute most to our current understanding of this protein family. The first chapters deal with the structure and function of the immunoglobulin molecule.

• antibody
• antigen
• immunoglobulin
• proteins

• Sloan-Kettering Institute for Cancer Research, Rye, USA

  Gary W. Litman

• Sloan-Kettering Institute for Cancer Research, New York, USA

  Robert A. Good

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