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IgG is a monomer composed of two heavy chains and two light chains of κ or λ.
It constitutes about 75% of the antibodies and is involved in neutralization, sedimentation and aggregation of toxins.
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The IgM molecule has ten heavy chains and light chains, as the basic structure of the five monomers consists of a circular array.
It is the first antibody to appear when the antigen enters, and it presents in the serum of the spinal animal.
It is because of IgM that aggregation occurs when different blood types are mixed in ABO blood type.
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IgA is present with two immunoglobulins attached, and it is found in the inner wall of the digestive canal or saliva such as respiratory mucus, saliva or tears, and is involved in infection defense on the mucosal surface.
The IgA concentration in various body fluids (such as the synovial fluid, spinal fluid, cerebrospinal fluid, ocular humor, etc.) is about 1/6 of IgG, but in secretion fluids (such as colostrum, respiratory mucus, intestinal mucus, saliva, etc.) it has much higher concentration than IgG or IgM, so it acts as the first line of defense against microbial invasion in the secreted fluid.
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IgD is a newly discovered immunoglobulin by discovering myeloma proteins in 1965. IgD also consists of two heavy chains and two light chains and it has fast coagulation rate and easily alter biological activity and structure.
It has been less known about the function of IgD, but it is known that it acts as a membrane receptor and involved in B cell maturation.
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IgE exists as a monomer and consists of two heavy chains and two light chains.
It exists the least in our body because it is bound to the cell membrane of certain cells, and is involved in allergic asthma, most adrenal infections, and allergic disease treatment.