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Only one type of light chain is present in a typical antibody, thus the two light chains of an individual antibody are identical. Each light chain is composed of two tandem immunoglobulin domains: one constant (C L) domain; one variable domain (V L) that is important for binding antigen; The approximate length of a light chain protein is from ...
Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
The light chain genes possess either a single (Cκ) or four (Cλ) Constant gene segments with numerous V and J gene segments but do not have D gene segments. [3] DNA rearrangement causes one copy of each type of gene segment to go in any given lymphocyte, generating an enormous antibody repertoire; roughly 3×10 11 combinations are possible ...
The multimeric structure of IgM is shown schematically in Figure 1. Figure 1A shows the "heterodimer" composed of one light chain, denoted L, and one heavy chain, denoted μ. The heavy and light chains are held together both by disulfide bonds (depicted as red triangles) and by non-covalent interactions.
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
Immunoglobulin E (IgE) is a type of antibody (or immunoglobulin (Ig) "isoform") that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains (ε chain) and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). [1]
Schematic diagram of a typical antibody showing two Ig heavy chains (purple) joined by disulfide bonds to two Ig light chains (green). The constant (C) and variable (V) domains are shown. An antibody molecule. The two heavy chains are colored red and blue and the two light chains green and yellow. [1]
Structure of a Fab with light and heavy chains. The fragment antigen-binding region (Fab region) is a region on an antibody that binds to antigens.It is composed of one constant and one variable domain of each of the heavy and the light chain.