Results 261 to 270 of about 62,488 (307)

Origins of immunoglobulin heavy chain domains

Journal of Molecular Evolution, 1980
Using 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.
W C, Barker, L K, Ketcham, M O, Dayhoff
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The immunoglobulin heavy chain class switch

Molecular and Cellular Biochemistry, 1984
While 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 ...
P D, Burrows, M D, Cooper
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HEAVY CHAINS OF MURINE SPLENOCYTE MEMBRANE IMMUNOGLOBULINS: A COMPARISON WITH THE HEAVY CHAINS OF HUMAN AND TOAD SERUM IMMUNOGLOBULINS

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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Regulation of immunoglobulin heavy‐chain gene rearrangements

Immunological Reviews, 2004
Summary:  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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Production of Antisera to the Heavy Chains of Chicken Immunoglobulins

British Veterinary Journal, 1983
A 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., Wilcox, G.E., Penhale, W.J.   +2 more
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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.
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Rat immunoglobulin E heavy chain locus

Journal of Molecular Biology, 1984
A 2100 base-pair long sequence has been established which covers all four constant domains of the rat epsilon-chain. An analysis of messenger RNA from an immunoglobulin E producing rat immunocytoma revealed two separate epsilon-chain mRNA species, 2.3 X 10(3) and 2.8 X 10(3) base-pairs long.
M L, Steen, L, Hellman, U, Pettersson
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Whale immunoglobulins—II. Heavy chain structure

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972
Abstract 1. 1. Immunoglobulins (7S) were purified from the plasmas of three species of whales, hump-backed, fin-backed and Sei. 2. 2. Heavy polypeptide chains were characterized and compared to human γ chains. 3. 3. Amino acid composition and peptide map comparisons indicated much homology between the whale 7S Ig heavy chain and hyman γ.
J C, Travis, B G, Sanders
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J Genes for Heavy Chain Immunoglobulins of Mouse

Science, 1980
A 15,8-kilobase pair fragment of BALB/c mouse liver DNA, cloned in the Charon 4Aλ phage vector system, was shown to contain the μ heavy chain constant region (C H μ) gene for the mouse immunoglobulin M. In addition, this fragment of DNA contains at least two J genes, used to code for the carboxyl terminal portion of
Newell, N, Richards, J E, Tucker, P W, Blattner, F R   +3 more
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Immunoglobulin heavy-chain constant-region genes

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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