Structure and function of immunoglobulins

Acta Endocrinol Suppl (Copenh). 1975;194:77-95. doi: 10.1530/acta.0.080s077.

Abstract

There are five major classes of immunoglobulins - IgG, M, A, D and E. Each is made of two heavy and two light chains or polymers of this basic subunit. The structure of each heavy and light chain consists of a variable region involved in antigen specificity and binding and a constant region which is involved in the class specific properties. The different classes of immunoglobulins differ in the biological properties. Of particular interest is the IgA fraction which provides antibodies in all the external secretions - including the reproductive organs. A few speculations are offered as to the possible role of IgA in reproductive biology.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibody Formation
  • Antibody Specificity
  • Binding Sites, Antibody
  • Epithelial Cells
  • Epithelium / immunology
  • Epitopes
  • Female
  • Humans
  • Immunoglobulin A
  • Immunoglobulin D
  • Immunoglobulin E
  • Immunoglobulin Fragments
  • Immunoglobulin G
  • Immunoglobulin M
  • Immunoglobulins*
  • Lymphoid Tissue / immunology
  • Male
  • Molecular Weight
  • Plasma Cells / immunology
  • Pregnancy
  • Reproduction

Substances

  • Epitopes
  • Immunoglobulin A
  • Immunoglobulin D
  • Immunoglobulin Fragments
  • Immunoglobulin G
  • Immunoglobulin M
  • Immunoglobulins
  • Immunoglobulin E