Results 361 to 370 of about 280,511 (396)
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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   +3 more
openaire   +3 more sources

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.
Bob G. Sanders, James C. Travis
openaire   +3 more sources

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.
Marie-Louise Steen   +2 more
openaire   +3 more sources

Organization of the Human Immunoglobulin Heavy-Chain Locus

1996
Immunoglobulin (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.
Fumihiko Matsuda, Tasuku Honjo
openaire   +3 more sources

Hv(1), a variable-region genetic marker of human immunoglobulin heavy chains.

Science, 1978
A new antigenic determinant was discovered with a hemagglutination-inhibition assay system. Designated Hv(1), it is located in the variable region of human immunoglobulin heavy chains of the G, M, and A classes.
A. Wang   +5 more
semanticscholar   +1 more source

Evolution of the Antarctic teleost immunoglobulin heavy chain gene

Molecular Phylogenetics and Evolution, 2010
Notothenioid teleosts underwent major modifications of their genome to adapt to the cooling of the Antarctic environment. In order to identify specific features of the Antarctic teleost immunoglobulin, transcripts encoding the constant region of the IgM heavy chain from 13 Antarctic and non-Antarctic notothenioid species were sequenced.
Coscia MR   +4 more
openaire   +5 more sources

Acquired potential N-glycosylation sites within the tumor-specific immunoglobulin heavy chains of B-cell malignancies.

Haematologica, 2004
BACKGROUND AND OBJECTIVES Among B-cell malignancies, follicular lymphomas (FL) more frequently show acquired, potential N-glycosylation sites (AGS) within tumor-specific immunoglobulin. The aim of this study was to extend this observation and to evaluate
N. Zabalegui   +9 more
semanticscholar   +1 more source

Reassembly of Immunoglobulin M Heavy and Light Chains In Vitro

Scandinavian Journal of Immunology, 1976
Reduced and alleviated monoclonal IgM was fractionated into μ and light (L) chains by gel chromatography in 1N acetic acid. Equimolar mixtures of the chains formed a noncovalently bonded structure in 0.01M sodium acetate buffer, pH 4.1, that had the properties of a half subunit.
R. B. Hester, R. E. Schrohenloher
openaire   +3 more sources

Effects of a long-term spaceflight on immunoglobulin heavy chains of the urodele amphibian Pleurodeles waltl.

Journal of applied physiology, 2005
A variety of immune parameters are modified during and after a spaceflight. The effects of spaceflights on cellular immunity are well documented; however, little is known about the effects of these flights on humoral immunity.
R. Boxio, C. Dournon, J. Frippiat
semanticscholar   +1 more source

Primary and secondary variants in immunoglobulin heavy chain production

Nature, 1976
WE have isolated numerous variants of a mouse myeloma cell line which synthesised altered heavy immunoglobulin chains and normal light chains after treating the line with the acridine mustard ICR-191 (refs 1–4). The four types of primary variants that we found are shown in Table 1.
Saija Koskimies   +2 more
openaire   +3 more sources

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