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The gamma globulins may be elevated (hypergammaglobulinemia), decreased (hypogammaglobulinaemia), or have an abnormal peak or peaks. Note that immunoglobulins may also be found in other zones; IgA typically migrates in the beta-gamma zone, and in particular, pathogenic immunoglobulins may migrate anywhere, including the alpha regions.
The high prevalence of IgA in mucosal areas is a result of a cooperation between plasma cells that produce polymeric IgA (pIgA), and mucosal epithelial cells that express polymeric immunoglobulin receptor (pIgR). [15] Polymeric IgA (mainly the secretory dimer) is produced by plasma cells in the lamina propria adjacent to
Hypergammaglobulinemia is a condition that is characterized by the increased levels of a certain immunoglobulin in the blood serum. [1] The name of the disorder refers to an excess of proteins after serum protein electrophoresis (found in the gammaglobulin region).
Immunoglobulin M (IgM) is the largest of several isotypes of antibodies (also known as immunoglobulin) that are produced by vertebrates.IgM is the first antibody to appear in the response to initial exposure to an antigen; [1] [2] causing it to also be called an acute phase antibody.
Selective immunoglobulin A (IgA) deficiency (SIgAD [1]) is a kind of immunodeficiency, a type of hypogammaglobulinemia. People with this deficiency lack immunoglobulin A (IgA), a type of antibody that protects against infections of the mucous membranes lining the mouth, airways, and digestive tract.
Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.
IgE that can specifically recognise an allergen (typically this is a protein, such as dust mite Der p 1, cat Fel d 1, grass or ragweed pollen, food protein, etc.) has a unique long-lived interaction with its high-affinity receptor FcεRI so that basophils and mast cells, capable of mediating inflammatory reactions, become "primed", ready to ...
In chickens, immunoglobulin Y is the functional equivalent to Immunoglobulin G (IgG). Like IgG, it is composed of two light and two heavy chains. Structurally, these two types of immunoglobulin differ primarily in the heavy chains, which in IgY have a molecular mass of about 65,100 atomic mass units (amu), and are thus larger than in IgG.