Results 351 to 360 of about 172,498 (401)
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Immunoglobulin heavy-chain switching in pre-B leukaemias
Nature, 1983Immunoglobulin gene expression is initiated in pre-B cells by rearrangements of heavy-chain variable genes V, D and J, for transcription together with the constant region gene C mu (refs 1-7). The subsequent joining of light-chain V-J genes in the kappa or lambda families leads to formation of complete IgM molecules, which are then expressed on the ...
H, Kubagawa +3 more
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Amino terminal sequences of human immunoglobulin heavy chains
Immunochemistry, 1971Abstract Partial amino-terminal sequences of 6γ, 5μ and 2α human Ig heavy chains not previously described, are presented. These sequences in conjunction with data on 28 other heavy chains permit further definition of heavy chain variable region subgroups.
A P, Kaplan +3 more
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J Genes for Heavy Chain Immunoglobulins of Mouse
Science, 1980A 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 +3 more
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Organization of the Human Immunoglobulin Heavy-Chain Locus
1996Immunoglobulin (Ig) heavy-chain (H) genes cluster at three loci in the human genome; the distal region of chromosome 14(1), chromosome 15(2) and chromosome 16(3). Among these only the chromosome 14 locus has been shown to generate a functional Ig gene by recombination of the variable (VH), diversity (D) and joining (JH) segments.
F, Matsuda, T, Honjo
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Immunoglobulin Heavy Chain Can Be Amyloidogenic
The American Journal of Surgical Pathology, 2003It is not well recognized that monoclonal immunoglobulin heavy chains or their fragments can be amyloidogenic. Amyloidosis due to heavy chains, referred to as AH amyloidosis, is rare with only three cases previously reported. An additional case of AH amyloidosis is reported.
Hoa L, Mai +4 more
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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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Biological variation of immunoglobulin heavy chain-light chain pairs in serum
Clinica Chimica Acta, 2014Assays for immunoglobulin heavy chain-light chain (HLC) pairs called Hevylite® have recently been developed. These assays can be useful in patients with hard to interpret serum protein electrophoresis peaks. Measurement of the biological variation of clinical laboratory tests can help clinicians better interpret laboratory results.Serum samples were ...
Judith A, Finlay, Alan H B, Wu
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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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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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Chapter 5 Immunoglobulin heavy chain class switching
1987Publisher Summary Whilst the variable region of an immunoglobulin molecule carries the antigen binding site and regulatory idiotypic determinants, the constant region is responsible for the effector functions of the molecule. These functions include transmembrane signalling and secretion signals, agglutination of antigens, complement activation and ...
U. Krawinkel, A. Radbruch
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Genetic control of variable and constant regions of immunoglobulin heavy chains.
Nature: New biology, 1971R. Mage, G. Young-Cooper, C. Alexander
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