An updated review on Immunoglobulin

Abstract

Immunoglobulin’s are heterodimeric proteins composed of two heavy (H) and two light (L) chains. They can be separated functionally into variable (V) domains that binds antigens and constant (C) domains that specify effectors functions such as activation of complement or binding to Fc receptors. The variable domains are created by means of a complex series of gene rearrangement events, and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation. Immunoglobulin is the antibodies and glycoprotein’s molecules produced by plasma cells or white blood cells, a signal production occur due the reaction with B cells. In 20th century the science of immunoglobulin was considered as an important science, centrifugation, Immuno adsorption such novel techniques was discovered for dissection of human blood components such as antibodies, so the naming of antibodies was necessary, Latin terms was used at that time for the purpose of naming. But the various in vitro studies shows that the pepsin and acidic condition shows a degradative effect on immunoglobulin neutralizing titer. To overcome this the IgY antibodies are encapsulated. For the protection of mucosal membrane of the IgA plays an essential role, the immune response of the secretory IgA is short lived due to this the genetically engineered antibodies are used for passive immunotherapy.