To use all functions of this page, please activate cookies in your browser.
my.chemeurope.com
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
Immunoglobulin GImmunoglobulin 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.[1] In birds, IgG is often called IgY, and is found in serum and yolk.[2] Additional recommended knowledge
FunctionsThis 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
Note: IgG affinity to Fc receptors on phagocytic cells is specific to individual species from which the antibody comes as well as the class. See alsoReferences
Categories: Glycoproteins | Antibodies |
||||||||||||||||||||||||||||||||||||||||||
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. |