Continuing education in immunology. I. The structure and function of immunoglobulins

Authors: Moriarty KM
Publication: New Zealand Veterinary Journal, Volume 32, Issue 5, pp 61-64, May 1984
Publisher: Taylor and Francis

Animal type: General
Subject Terms: Biochemistry/chemistry, Clinical pathology, Diagnostic procedures, Education/communication, Immune system/immunology, Nutrition/metabolism, Protein
Article class: General Article

---

Abstract: INTRODUCTION: When an immune serum is fractionated into its major components, for example by electrophoresis, the bulk of its antibody activity is seen to occur in the gamma globulins with some slight additional activity in the beta globulins. Proteins that have antibody activity are called immunoglobulins; these are divided into classes which differ in their structure and biology. Five such classes, designated IgG, IgM, IgA, IgD, and IgE, have been described in man. Immunoglobulins analogous to those of man probably occur in all mammals but in most species they remain to be specifically identified. Furthermore, the features of a given immunoglobulin class are broadly the same regardless of the species in which it occurs. Antibodies are involved in two types of activity. The first of these is their specific reaction with antigen; the second is a consequence of this and involves the molecules in non-specific effector functions such as complement fixation and attachment to phagocytic cells. These two activities are associated with different parts of the antibody molecule and to understand them we must know something of the structure of immunoglobulins. This article describes the structure of the prototypical IgG molecule, a structure which, with very little modification, is common to all immunoglobulins.

---