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Structure of immunoglobulins

Francisco A Bonilla, MD, PhD
Section Editor
E Richard Stiehm, MD
Deputy Editor
Anna M Feldweg, MD


Immunoglobulin molecules are multifunctional tools used by cells to mediate interactions of antigen molecules with a variety of cellular and humoral effector mechanisms. The effector mechanisms include activation of the following systems: signal transduction machinery in the B cell cytoplasm (in the case of surface immunoglobulin receptors), receptors for the constant region of immunoglobulin G (IgG), and the complement system. They also play a role in the afferent limb of the immune system both through antigen presentation and by interacting with regulatory receptors on immune cells.

The basic aspects of immunoglobulin structure will be reviewed here. A discussion of their function, the derivation of monoclonal antibodies, and the various laboratory and clinical applications of immunoglobulin reagents is presented separately. (See "Overview of therapeutic monoclonal antibodies".)


Four-chain unit — The immunoglobulin molecule contains four separate polypeptides (figure 1):

Two identical light (L) chains of molecular weight (MW) 23 kilodaltons (kd)

Two identical heavy (H) chains of MW around 55 kd

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Literature review current through: Nov 2017. | This topic last updated: Jun 06, 2016.
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