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Immunoglobulin G (IgG) is a multimeric immunoglobulin, built of two heavy chains γ 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.
In birds, IgG is often called IgY, and is found in serum and yolk.
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.
Note: IgG affinity to Fc receptors on phagocytic cells is specific to individual species from which the antibody comes as well as the class.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Immunoglobulin_G". A list of authors is available in Wikipedia.|