Immunoglobulin G

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Molecular surface of an IgG molecule

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Overview

Immunoglobulin G (IgG) is a multimeric immunoglobulin, built of two heavy chains Failed to parse (MathML with SVG or PNG fallback (recommended for modern browsers and accessibility tools): Invalid response ("Math extension cannot connect to Restbase.") from server "https://api.formulasearchengine.com/v1/":): \gamma and two light chains. Each complex has two antigen binding sites. This is the most abundant immunoglobulin and is approximately equally distributed in blood and in tissue liquids, constituting 75% of serum immunoglobulins in humans.[1]

In birds, IgG is often called IgY, and is found in serum and yolk.[2]

Functions

This is the only isotype that can pass through the human placenta, thereby providing protection to the fetus in its first weeks of life before its own immune system has developed.

It can bind to many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body against them by complement activation (classic pathway), opsonization for phagocytosis and neutralisation of their toxins.

IgG can cause food allergy, and in such causes delayed-onset food allergy, in contrast to food allergy by IgE, whose effects appear rapidly.

Subclasses

Name Percent Crosses placenta easily Complement activator Binds to Fc receptors on phagocytic cells
IgG1 66% yes second highest high affinity
IgG2 23% no third highest extremely low affinity
IgG3 7% yes highest high affinity
IgG4 4% yes no intermediate affinity

Note: IgG affinity to Fc receptors on phagocytic cells is specific to individual species from which the antibody comes as well as the class.

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References

  1. Junqueira, Luiz C. (2003). Basic Histology. McGraw-Hill. ISBN 0838505902.  Unknown parameter |coauthors= ignored (help)
  2. http://www.sigmaaldrich.com/Brands/Sigma_Genosys/Custom_Antisera/Key_Resources/Antisera_FAQ/Chicken_Antibody.html
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