scholarly journals Ig Kappa Chain V-IV Region

2020 ◽  
Author(s):  
Keyword(s):  
Kappa Chain

Kappa chain structure from a crystallized murine Fab′: Role of joining segment in hapten binding

1981 ◽  
Vol 18 (8) ◽  
pp. 705-711 ◽  
Author(s):  
S RUDIKOFF ◽  
Y SATOW ◽  
E PADLAN ◽  
D DAVIES ◽  
M POTTER
Keyword(s):  
Chain Structure ◽  
Kappa Chain

scholarly journals The active immunoglobulin kappa chain gene is packaged by non-ubiquitin-conjugated nucleosomes.

1986 ◽  
Vol 83 (11) ◽  
pp. 3738-3742 ◽  
Author(s):  
S. Y. Huang ◽  
M. B. Barnard ◽  
M. Xu ◽  
S. Matsui ◽  
S. M. Rose ◽  
...  
Keyword(s):  
Chain Gene ◽  
Immunoglobulin Kappa ◽  
Kappa Chain

Improved clonality detection in Hodgkin lymphoma using the BIOMED-2-based heavy and kappa chain assay: a paraffin-embedded tissue study

2012 ◽  
Vol 60 (5) ◽  
pp. 768-773 ◽  
Author(s):  
Gustavo Tapia ◽  
Carolina Sanz ◽  
José L Mate ◽  
Ana M Muñoz-Mármol ◽  
Aurelio Ariza
Keyword(s):  
Hodgkin Lymphoma ◽  
Kappa Chain

kappa/lambda index for confirming urinary free light chain in amyloidosis AL and other plasma cell dyscrasias

1991 ◽  
Vol 37 (6) ◽  
pp. 1122-1126 ◽  
Author(s):  
Stanley S Levinson
Keyword(s):  
Plasma Cell ◽  
Electrophoretic Pattern ◽  
Light Chains ◽  
Plasma Cell Dyscrasia ◽  
Serum Samples ◽  
Kappa Chain ◽  
Immunofixation Electrophoresis ◽  
Patient Groups ◽  
Bone Marrow Analysis ◽  
Serum And Urine

Abstract Primary systemic amyloidosis (AL), a disease involving the deposition of immunoglobulin light chains in tissue, is caused by a plasma cell dyscrasia. In the case of amyloidosis reported here, no monoclonal component was seen upon routine protein electrophoresis of serum or urine nor was a bone marrow analysis positive for AL. Immunofixation electrophoresis did not show a typical paraprotein band but did show, in the gamma region, two large diffuse bands and a lower concentration of oligoclonal-type bands, all of which stained for free lambda but not for free kappa chain. The ratio of kappa to lambda chains in urine was 0.178, much less than the ratio in serum (1.3). Six other urine samples from a group of patients with documented Bence Jones proteinuria also exhibited kappa/lambda ratios that differed manyfold from the ratios in their corresponding serum samples. On the other hand, the kappa/lambda ratios from seven controls (seven patients with generalized proteinuria unrelated to plasma cell dyscrasia) were similar in serum and urine. This difference between the kappa/lambda ratios from serum and urine can be expressed as a kappa/lambda index. The index was significantly different (P less than 0.01) between the two patient groups compared here, and was useful in confirming the presence of Bence Jones protein in this case with a difficult-to-interpret electrophoretic pattern. Although the kappa/lambda ratio has been widely used for confirmation and identification of monoclonal components in serum, its use in clinical laboratories has not been widely extended to urine. Comparison of serum and urine kappa/lambda ratios as a kappa/lambda index may help reduce the need for more complex immunoelectrophoresis techniques in identifying free light chains in urine.

scholarly journals Structural analysis of the human immunodeficiency virus-binding domain of CD4. Epitope mapping with site-directed mutants and anti-idiotypes.

1989 ◽  
Vol 170 (4) ◽  
pp. 1319-1334 ◽  
Author(s):  
Q J Sattentau ◽  
J Arthos ◽  
K Deen ◽  
N Hanna ◽  
D Healey ◽  
...  
Keyword(s):  
Epitope Mapping ◽  
Lymphocyte Activation ◽  
Vaccine Strategy ◽  
Virus Binding ◽  
Linear Sequence ◽  
Kappa Chain ◽  
High Affinity Binding Site ◽  
Glycoprotein Gp120 ◽  
Differentiation Marker ◽  
Hiv Envelope

The CD4 molecule, a differentiation marker expressed primarily by T lymphocytes, plays an important role in lymphocyte activation. CD4 is also the receptor for HIV. A number of recent studies have localized the high affinity binding site of the HIV envelope glycoprotein, gp120, to the NH2-terminal (V1) domain of CD4, a region with sequence and predicted structural homology with Ig kappa chain V domains (V kappa). In this report, we show that V1 bears structural similarities with V kappa regions through detailed epitope mapping of 26 CD4 mAbs. The binding sites of these mAbs were initially defined relative to one another by crossblocking analysis and were then localized to specific domains of CD4 in blocking studies with truncated, soluble CD4 proteins. The epitopes within the V1 domain were mapped in detail with a panel of 17 substitution mutants, and the specificities of several mAbs that appear to recognize very similar epitopes were examined in crossblocking studies with anti-idiotype antibodies. The location of the epitopes is consistent with a V kappa-like structure of V1. Most of the epitopes lie within regions of predicted exposed loops. A number of these epitopes span discontinuous residues in the linear sequence that lies in close proximity in an Ig fold. Alignment of CD4 V1 with the Ig V kappa chains places these epitopes within stretches corresponding to the complimentarity-determining regions. This epitope analysis is relevant for a vaccine strategy for HIV based on anti-idiotype antibodies to CD4 mAbs and for studies with CD4 antibodies on the role of CD4 in T lymphocyte activation.

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