Discuss the specific properties of the 5 classes of Immunoglobulins and the specific component parts that each have (i.e., J chain, SC protein, CDR regions, ITAM regions, complement activation, allotype variation). Solution Generally there are 5 classes of immunoglobins, and they are IgG, IgM,IgA, IgD and IgE. IgG It is the major immunoglobin present in the serum almost about 75 % of immunoglobin in serum is IgG. Its an important antibody in secondary immune response. It promotes opsonization and fixes complement and also enhances phagocytosis. IgM It is the third most common immunoglobin in the serum. It is the first immunoglobin to be made by the fetus. It has a pentameric structure. The pentamer has a J chain. Most capable of complement fixation, agglutination. Present mainly on B cells and effective against viruses and bacteria. IgM have about 60 CDR’s. IgA Secretory immunoglobin mainly present in tears, saliva, colostrum and helps in removal of microbes from mucous membrane. Consist of 2 heavy chains and two light chains joined by a J chain. It does not fix complement. Colostrum is having abundant IgA. SC protein is a part of IgA. IgD Present in low levels in serum and found on B cell surface. Exist as monomers. Complement binding is not done by IgD. The exact function of this class is still not known precisely. IgE Monomeric in nature and least amounts are present. Responsible for allergic reactions. Present in skin and lungs. Do not fix complement. Effective against parasites in the body. Commonly related to diseases like asthma. CDR’s: Except IgM all other antibodies have 12 CDR’s. Since IgM is a pentameric molecule it has about 60 CDR’s. ITAM regions: These are motifs present in the Fc receptors of immunoglobin molecule. Allotype: Allele of the antibody chains is termed as allotype..