light chain


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Related to light chain: Myosin light chain kinase

chain

 [chān]
a collection of objects linked together in linear fashion, or end to end, as the assemblage of atoms or radicals in a chemical compound, or an assemblage of individual bacterial cells.
branched chain an open chain of atoms, usually carbon, with one or more side chains attached to it.
closed chain several atoms linked together so as to form a ring, which may be saturated, as in cyclopentane, or aromatic, as in benzene.
H chain (heavy chain) any of the large polypeptide chains of five classes that, paired with the L or light chains, make up the antibody molecule of an immunoglobulin; heavy chains bear the antigenic determinants that differentiate the classes of immunoglobulins. See also heavy chain disease.
J chain a polypeptide occurring in polymeric IgM and IgA molecules.
L chain (light chain) either of the two small polypeptide chains (molecular weight 22,000) that, when linked to H or heavy chains by disulfide bonds, make up the antibody molecule of an immunoglobulin monomer; they are of two types, kappa and lambda, which are unrelated to immunoglobulin class differences.
open chain a series of atoms united in a straight line; components of this series are related to methane.
chain reaction a chemical reaction that is self-propagating; each time a free radical is destroyed a new one is formed.
side chain a group of atoms attached to a larger chain or to a ring.

light chain

a polypeptide chain of low molecular weight, such as the κ or λ chains in immunoglobulin. There are two identical κ- or λ-light chains in each immunoglobulin monomer.
Synonym(s): L chain

light chain

n.
The smaller of the two types of polypeptide chains in immunoglobulins, consisting of an antigen-binding portion with a variable amino acid sequence, and a constant region with an amino acid sequence that is relatively unchanging.

light chain

(līt chān)
A polypeptide chain with low molecular weight, as the κ or λ chains in immunoglobulin.

light chain

see IMMUNOGLOBULIN.
References in periodicals archive ?
If an apparent monoclonal band only reacts with antisera to either [kappa] or [lambda] light chain (and not to [gamma], [alpha], or [mu] heavy chain), does your laboratory perform or suggest additional testing to verify that it is a monoclonal free light chain (and not a monoclonal IgD or IgE immunoglobulin)?
In meat samples, the main protein bands identified in the range of molecular weights from 250 to 10kDa were myosin heavy chain (MHC), [alpha]-actinin ([alpha]-act), desmin, actin (ACT), troponin T (TnT), tropomyosin (TPM), myosin light chains 1 (MLC1), troponin C (TnC), and myosin light chains 2 (MLC2).
Fluorescent immunostaining of IgA subtypes and light chains showed positive staining for IgA1 and k light chains, while staining for IgA2 and A light chains was negative.
The remaining M[alpha]F-Ig mAb (4-E3, 4-D11, and 6-H5) also had light chain reactivity.
Although the use of two separate vectors for the expression of heavy chain and light chain has been reported, this approach has serious shortcomings such as the possibility of the integration of the two vectors in different genomic sites and the variation of the copy number for each gene which can in turn cause an improper ratio of the expressed light chain to heavy chain, and reduce the possibility of achieving cell clones with high expression level of active antibody.
Extended use of serum free light chain as a biomarker in lymphoproliferative disorders: a comprehensive review.
Background: Light chain (LC) and heavy chain carboxyterminal subdomain ([H.sub.CC]) fragments are the most important parts of tetanus neurotoxin (TeNT) which play bey roles in toxicity and binding of TeNT, respectively.
For antibodies intended for therapeutic use or sequencing the N-terminals of the heavy chain and the light chain using protein sequencing methods to confirm the cDNA sequences cloned from hybridoma cell lines, you can contact info@Creative-Biolabs.Com or call 1-631-871-5806.
Serum and urine protein electrophoresis did not reveal paraproteinemia, and quantitative serum immunoglobulin and serum free light chain (FLC) assays did not reveal light chain restriction or excess.
An increased free light chain concentration has been reported in a variety of inflammatory and autoimmune diseases and reflects the polyclonal B lymphocytes activation in these pathologies.
The myosin molecule has the IQ motif sequence in the neck for binding the light chain, (16) but the IQ motif is a calmodulin binding site in the [Ca.sup.++]-independent manner.