Encyclopedia of Behavioral Medicine

2013 Edition
| Editors: Marc D. Gellman, J. Rick Turner


  • Joanna Long
Reference work entry
DOI: https://doi.org/10.1007/978-1-4419-1005-9_465



Immunoglobulins (Igs) are a subclass of antibodies which are produced in the early stages of B-cell development (Abbas & Lichtman, 2006). The structure of Igs can differ between class types; however, they are built from a number of the same basic units known as immunoglobulin domains (Fig. 1). These are formed from 110 similar, but not identical, amino acid sequences which fold to form a globular structure. Each Ig is composed of two identical myosin heavy chain and two identical myosin light chain units, connected by a number of disulfide bonds. The Fab region is where different antigens bind to depending on the Ig subtype and is known as the antigen binding site. The first immunoglobulin domain possesses a large variability of amino acid sequences which determine the antigen-binding specificity of the antibody molecule, thus allowing great diversity of antigen recognition. The hinge region allows some flexibility of the molecule when binding with...
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References and Readings

  1. Abbas, A. K., & Lichtman, A. H. (2006). Basic immunology: Functions and disorders of the immune system (2nd ed.). Philadelphia: Elsevier.Google Scholar
  2. Newsholme, E., & Leech, T. (2010). Functional biochemistry in health and disease (2nd ed.). Chichester: Wiley-Blackwell.Google Scholar

Copyright information

© Springer Science+Business Media, New York 2013

Authors and Affiliations

  1. 1.School of Sport and Exercise SciencesUniversity of BirminghamEdgbaston, BirminghamUK