Light chains
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Two light chains are either κ (Kappa) or λ (lambda) but never both in one immunoglobulin.
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The names were derived from Koragold (κ) and Lapori (λ) who originally described. Each light chain consists of two domains of 110 amino acids.
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The amino acid sequence of C-terminus domain is constant (CL) where as sequence of N-terminus is variable (VL) and some regions show great variability, known as hyper variable regions or complementarity determining regions (CDRs) or hot spots, each containing 6-10 amino acids. Between the CDRs there are intervening peptide sequences called frame work regions.
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Three regions show maximum variability i.e. at position 24-34, 50 to 56 and 89-97.
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The amino acid sequence in VL domain of each light chain is different. Molecular weight of each light chain is 25KDa.
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The presence of κ or λ light chain varies with species. For example, cattle and horses have 95 % λ, rat and mice have over 95 % κ chain, monkeys have 50 % of each and humans have 60 % κ chains.
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Last modified: Friday, 23 September 2011, 10:38 AM