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Schematic diagram of an typical antibody showing two Ig heavy chains (blue) linked 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. See also:[1] A light chain is the small polypeptide subunit of an antibody (or immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.
[edit] In humansThere are two types of light chain in mammals,
Antibodies are produced by B lymphocytes which each express only one class of light chain. Once set, light chain class remains fixed for the life of the B lymphocyte. In a healthy individual, the total kappa to lambda ratio is roughly 65 to 35, with a highly divergent ratio indicative of neoplasm. [edit] In other animalsThe immunoglobulin light chain genes in tetrapods can be classified into three distinct groups: kappa (κ), lambda (λ), and sigma (σ). The divergence of the κ, λ, and σ isotypes preceded the radiation of tetrapods. The σ isotype was lost after the evolution of the amphibian lineage and before the emergence of the reptilian lineage.[1] Other types of light chains can be found in lower vertebrates, such as the Ig-Light-Iota chain of Chondrichthyes and Teleostei.[2][3] Camelids are unique among mammals as they have fully functional antibodies which have two heavy chains, but lack the light chains usually paired with each heavy chain.[4] The functional role of this separate repertoire is unknown as yet. [edit] StructureOnly 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:
The approximate length of a light chain protein is from 211 to 217 amino acids.[2] [edit] In pathologyIg light chains produced in neoplastic plasma cells, e.g. in multiple myeloma, are called Bence Jones proteins. [edit] References
[edit] External links
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