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Immunohistochemical study of immunoglobulin light chain amyloidosis with antibodies to the immunoglobulin light chain variable region

Pathology International, 2006
To detect immunoglobulin (Ig) light chain amyloidosis (AL amyloidosis) in formalin‐fixed, paraffin‐embedded tissue sections by immunohistochemistry, polyclonal antibodies were generated against synthetic peptides corresponding to amino acids 1–19 of the Ig λ light chain V λ VI subgroup (anti‐V λ VI (1–19)) and the Ig κ light chain Vκ I subgroup (anti ...
Yoshinobu, Hoshii   +4 more
openaire   +2 more sources

The origin of light and heavy chains of immunoglobulins

Biochemical and Biophysical Research Communications, 1971
Abstract A model is proposed for the origin of H chains of Ig by the translocation of vc1 gene for light chains to a c2c3 gene giving rise to a vc1c2c3 gene. This explains why the common part of H chain is three times longer than the variable part.
openaire   +2 more sources

Immunoglobulin Light Chain and Systemic Light-Chain Amyloidosis

2007
Light-chain amyloidosis (AL) is characterized by the clonal expansion of plasma B cells that secrete large amounts of monoclonal immunoglobulin light chains. The free light chains circulate in serum and form amyloid fibrils on vital organs such as the kidney, heart, and liver causing organ failure and eventually death.
Marina Ramirez-Alvarado   +5 more
openaire   +1 more source

Abnormal immunoglobulin synthesis in monoclonal immunoglobulin light chain and light and heavy chain deposition disease

Amyloid, 2001
The Congo red-binding fibrils of AL amyloidosis are the most common form of monoclonal immunoglobulin tissue deposition (MIDD). Nonetheless, the less structured deposits found in light chain deposition disease (LCDD) and the similar, but distinct, deposits of light and heavy chain deposition disease (LHCDD) and heavy chain deposition disease (HCDD) can
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RL allotypes of light chains of rat immunoglobulins

Immunochemistry, 1971
Abstract Allotypes of rat immunoglobulins have been detected by using the inhibition of immunoadsorption of iodinated rat immunoglobulin G on corresponding antibodies fixed on cellulose. The observed allotypic differences between the immunoglobulins of inbred rat strains—strain MSUB1 on the one hand and rat strains WAG and August on the other are due
O V, Rokhlin   +2 more
openaire   +2 more sources

Structural landscape of immunoglobulin lambda light chains

Proceedings of the First ACM International Conference on Bioinformatics and Computational Biology, 2010
The immunoglobulin lambda isotype family is present in nearly all vertebrates and plays a primary role in the human immune system. Despite its importance, few if any systematic studies have been performed to identify, as it has been the case for kappa and heavy chains, a set of structural conformations adopted by the loops forming its Antigen Binding ...
CHAILYAN, ANNA   +3 more
openaire   +2 more sources

Shared epitopes of avian immunoglobulin light chains

Veterinary Immunology and Immunopathology, 2014
Like all jawed vertebrates, birds (Aves) also produce antibodies i.e. immunoglobulins (Igs) as a defence mechanism against pathogens. Their Igs are composed of two identical heavy (H) and light (L) chains which are of lambda isotype. The L chain consists of variable (VL), joining (JL) and constant (CL) region.
Mateja, Benčina   +5 more
openaire   +2 more sources

Immunoglobulin Light Chain Genes

1987
The immunoglobulin genes are built from variable, joining, and constant gene segments (V, J, C). The V and J+C gene segments are separate in germline DNA and are brought into close proximity in the immunoglobulin-producing lymphoid cells. Antibody diversity rests mainly on the existence of many different V and several different J gene segments, on the ...
H. G. Zachau   +6 more
openaire   +1 more source

Immunoglobulin light chain nephropathies.

Pathology annual, 1987
Excessive monoclonal light chain production and excretion may result in a variety of renal diseases which may collectively or individually be referred to as light chain nephropathy. Kappa light chains are more likely to produce tubular dysfunction and nodular nonamyloidotic glomerulosclerosis, while lambda light chains are more likely to be involved in
B C, Sturgill, F L, Tucker, W K, Bolton
openaire   +1 more source

Lambda light chains in rat immunoglobulins

Immunochemistry, 1973
P, Ouerinjean   +5 more
openaire   +2 more sources

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