Discussion of all aspects of cellular structure, physiology and communication.
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Not exactly sure what the question is. There are 5 types of heavy chains, one for each of the classes of immunoglobulins: IgM, IgG, IgD, IgA, and IgE. Each type of heavy chain has a distinct set of cystine cross-links.
A protein of animal origin with known antibody activity. Immunoglobulins are major components of what is called the humoral immune response system. They are synthesized by lymphocytes and plasma cells and found in the serum and in other body fluids and tissues, including the urine, spinal fluid, lymph nodes, and spleen. Each immunoglobulin molecule consists of four polypeptide chains: two heavy chains (H chains) and two light chains (L chains). There are five antigenically different kinds of H chains, and this difference is the basis for the classification of immunoglobulins. The five major classes of immunoglobulins (Ig) are IgA, IgD, IgE, IgG, and IgM. (See accompanying figure.) Each class varies in its chemical structure and in its number of antigen-binding sites and adheres to and reacts only with the specific antigen for which it was produced.
Immunoglobulin, also known as antibody, which produced by plasma cells , is a large Y-shape protein. There are five isotypes in placental mammals, which are IgA, IgD, IgE, IgG, and IgM. The immune system, which is highly complex and exceedingly specific, uses these glycoprotein molecules to identify and neutralize particular antigens, such as bacteria and viruses.
Immunoglobulin acts as a critical part of the immune response by specifically recognizing and binding to foreign objects, such as bacteria or viruses and aiding in their destruction. The various immunoglobulin isotypes differ in their biological features, structures, target specificity and distribution. Hence the assessment of the immunoglobulin isotype can provide useful insight into complex humoral immune response.
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