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Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin epsilon (IgE) exists as a monomer. The IgE heavy chain is an e chain, and the light chains are either k- or l- chains. IgE is significantly involved in the allergic response of the body. It binds to receptors on the surface of basophils, mast cells and activated eosinophils. One dominant functional activity of IgE is the sensitization of mast cells. IgE binds to the Fc e RI receptor on the surface of mast cells, causing the cell to release chemicals that induce reactions such as sneezing and coughing. IgE also helps to protect the host against large parasites. It coats the surface of the parasite attracting eosinophils via the Fc e RI receptor. The eosinophils can then attack the parasites that are too large to be ingested by phagocytes.
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