Note on immunoglobulin protein structure and its types

Perspective - (2022) Volume 9, Issue 1

War D. Mi*
*Correspondence: War D. Mi, Department of Immunology, Harvard University, Cambridge, USA, Email:
Department of Immunology, Harvard University, Cambridge, USA

Received: 03-Mar-2022, Manuscript No. AJIROA-22-56210; Editor assigned: 05-Mar-2022, Pre QC No. AJIROA-22-56210 (PQ); Reviewed: 19-Mar-2022, QC No. AJIROA-22-56210; Revised: 24-Mar-2022, Manuscript No. AJIROA-22-56210 (R); Published: 31-Mar-2022


Immunoglobulins, also known as antibodies, are glycoprotein molecules produced by plasma cells. They act as an important part of the immune response by detecting and binding to certain antigens, such as viruses or bacteria, and aiding in their destruction. The immunoglobulin compound, also known as immunoglobulin fold, is a type of protein compound containing a 2-component sandwich 7-9 antiparallel β-strands arranged in two β sheets with Greek key topology, consisting of approximately 125 amino acids. The ability of this Fc clip to bind to complement or Fc receptors but not to the antigens allowed to map the antibody effect function in this area. The antibody phase that works by its function is determined only by the composition of its HC. The use of protease pepsin allowed the identification of F-fraction. The storage of the disulfide bond that binds the two HCs results in a fragment containing both regions of Fab, making it bivalent and capable of stabilizing and binding antigen. The same specification of the two Fab regional antigens allows antigen-mediated linking and is essential for BCR-directed activation of B cells and the immune function of the immune system. There are several types of Immunoglobulin.


Immunoglobulin G: Immunoglobulin G is a type of antibody. Representing about 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. IgG molecules are synthesized and secreted by plasma B cells. Each IgG antibody contains two parasites.

Immunoglobulin M: Immunoglobulin M is one of several antibody isotypes also known as immunoglobulin produced by vertebrates. IgM is the largest antibody, and is the first antibody to respond to initial exposure to antigen.

Immunoglobulin A: Immunoglobulin A is an antibody that plays a key role in the humans immune system. The amount of IgA produced in combination with mucous membranes is greater than all other antibody compound combined. In absolute terms, between 3 and 5 grams are injected into the intestinal tract each day.

Immunoglobulin D: Immunoglobulin D is an antibody isotype that makes up about 1% of the proteins in the plasma membrane of immature B-lymphocytes where it is normally produced and another antibody surface called IgM. IgD is also secreted by secretions found in very small amounts in blood serum, representing 0.25% of immunoglobulins in serum. The relative cell weight and half-life of IgD secretory is 185 kDa and 2.8 days, respectively. Secreted IgD is produced as a monomeric antibody with two heavy delta (δ) class chains, as well as two Ig light chains. The work of IgD has been a mystery in immunology since its discovery in 1964. IgD is present in a variety of fish from cartilaginous to humans excluding possible birds. This ubiquitous manifestation of mutations in the immune system suggests that IgD may be as old as IgM and suggests that IgD has important immune functions.

In B cells, the function of IgD is to indicate that B cells will be opened. By activation, B cells are ready to participate in the immune system as part of the immune system. During B cell division, IgM is a special isotype expressed by immature B cells. IgD begins to develop when a B cell breaks out of the bone marrow to fill the peripheral lymphoid tissue.

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