Results 351 to 360 of about 280,511 (396)
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Addition of glucosamine and mannose to nascent immunoglobulin heavy chains
Biochemistry, 1977We have investigated the process of protein glycosylation in an attempt to answer the question of whether glucosamine and mannose are added to nascent chains prior to chain completion or only to completed chains after release from the ribosome. The MPC 11 mouse plasmacytoma cell line used in these studies synthesizes a glycosylated gamma2b heavy chain ...
W. M. Kuehl, L. W. Bergman
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The immunoglobulin heavy chain class switch
Molecular and Cellular Biochemistry, 1984While much has been learned concerning the molecular structural basis for the heavy chain class switch, many questions relating to the regulation of the switch remain unanswered, or at least controversial. Identification of the enzyme system which mediates the class switch, as well as other regulatory, possibly X-linked, genes should provide the ...
Max D. Cooper, Peter D. Burrows
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Origins of immunoglobulin heavy chain domains
Journal of Molecular Evolution, 1980Using computer programs that analyze the evolutionary history and probability of relationship of protein sequences, we have investigated the gene duplication events that led to the present configuration of immunoglobulin C regions, with particular attention to the origins of the homology regions (domains) of the heavy chains.
Winona C. Barker +2 more
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Immunoglobulin heavy chain binding protein
Nature, 1983Pre-B lymphocytes, and hybridomas derived from them, synthesize immunoglobulin heavy (IgH) chain in the absence of light (L) chain. In the Abelson virus transformed line 18-81, which is representative of the pre-B cell stage, we observed that at least some of the H-chains are bound to a protein other than L-chain.
Ingrid G. Haas, Matthias Wabl
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International Journal of Immunogenetics, 1976
SUMMARYThe mobilities of murine splenocyte surface immunoglobulin heavy chains were compared by polyacrylamide gel electrophoresis in SDS‐containing buffers, with those of the heavy chains of human IgM, IgG, and IgD, and toad IgY. Human δ‐chain showed a mobility only slightly faster than that of human μ‐chain, and required double‐labelling techniques ...
Warr, G W, Marchalonis, J J
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SUMMARYThe mobilities of murine splenocyte surface immunoglobulin heavy chains were compared by polyacrylamide gel electrophoresis in SDS‐containing buffers, with those of the heavy chains of human IgM, IgG, and IgD, and toad IgY. Human δ‐chain showed a mobility only slightly faster than that of human μ‐chain, and required double‐labelling techniques ...
Warr, G W, Marchalonis, J J
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Production of Antisera to the Heavy Chains of Chicken Immunoglobulins
British Veterinary Journal, 1983A number of attempts made to raise monospecific antiserum against chicken immunoglobulin G in rabbits by conventional methods employing immunization with various whole IgG preparations, and complete Freund’s adjuvant resulted in antisera which showed reactivity predominantly against light chains.
Nandapalan, N. +2 more
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The role of immunoglobulin heavy chain binding protein
Immunology Today, 1987More than ten years ago a heavy chain binding protein (BiP) was described which is associated with immunoglobulin heavy chains (HC) within the endoplasmic reticulum (ER) [which is the site of Immunoglobulin (Ig) assembly]. Recently, Linda Hendershot and her collegues suggested that BiP might combine with nascent HC as they enter the ER and hold them ...
Linda Hendershot +2 more
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Regulation of immunoglobulin heavy‐chain gene rearrangements
Immunological Reviews, 2004Summary: Regulated assembly of antigen receptor gene segments to produce functional genes is a hallmark of B‐ and T‐lymphocyte development. The immunoglobulin heavy‐chain (IgH) and T‐cell receptor β‐chain genes rearrange first in B and T lineages, respectively.
Dipanjan Chowdhury, Ranjan Sen
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Immunoglobulin heavy-chain constant-region genes [PDF]
Cell, 1982 Antibodies are composed of two identical heavyand light-chain polypeptides. Each heavy and light chain contains an amino-terminal variable (V) region, responsible for antigen recognition, and a carboxy-proximal constant(C) region, which participates in a variety of immunological processes, including effector-cell recognition and complement fixation ...
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The origin of light and heavy chains of immunoglobulins
Biochemical and Biophysical Research Communications, 1971Abstract 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.
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