Results 161 to 170 of about 218 (190)

Mutual homology of mouse immunoglobulin .gamma.-chain gene sequences

Biochemistry, 1979
We have assessed the relative homology of mouse immunoglobulin heavy-chain gene sequence using complementary DNAs (cDNAs) synthesized against gamma-chain mRNAs (gamma 1, gamma 2a, gamma 2b, and gamma 3) purified from mouse myelomas. cDNAs complementary to the gamma-chain mRNAs did not cross-hybridize with the mu- and alpha-chain mRNAs, whereas they ...
Yamawaki, kataoka Y, Sato, K, Shimizu, A, Kataoka, T, Mano, Y, Ono, M, Kawakami, M, Honjo, T   +7 more
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Structure of mink immunoglobulin γ chain cDNA

Developmental & Comparative Immunology, 1996
Two cDNA clones, encoding mink Ig gamma chains were characterized. The pIGG47 clone contains a part of the leader segment, VDJ and C regions, and pIGG14 contains a part of the J and a complete C region. The clones differ by only four nucleotides in the C region, and they most probably represent allelic variants of the same gene.
Najakshin, A. M., Belousov, E. S., Alabyev B. Y. u.,, Christensen, J., Storgaard, T., Aasted, B., Taranin, A.   +6 more
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Genetic control of gamma chain synthesis: A chemical and evolutionary study of the Gm(a) factor of immunoglobulins

Journal of Molecular Biology, 1969
Abstract The amino acid sequences of the Gm“a” peptide, the Gm“non-a” peptide and the OWM peptide of immunoglobulins have been elucidated. The results indicate that both the a and non-a peptides in humans and higher apes were evolutionarily derived from the OWM peptide in the Old World Monkeys by single-step point mutations.
H. Hugh Fudenberg, An-Chuan Wang
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Subclasses of porcine immunoglobulins G. Production of subclass specific antisera with S‐sulfonated gamma chains

European Journal of Immunology, 1972
AbstractUsing antisera made against porcine S‐sulfonated heavy chains two subclasses of porcine IgG could be distinguished on the basis of antigenic determinants located on the Fc fragment. The antisera prepared against the porcine gamma chains reacted with other mammalian IgG proteins, but not with avian, amphibian or fish immunoglobulins.
Jean-Jacques Metzger, Monique Houdayer
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A note on the amino acid sequence of residues 381–391 of human immunoglobulin gamma chains

Molecular Immunology, 1979
Abstract The amino acid sequence of residues 381–;391 of the γ-chain of IgG2 Zie has been determined. It is Trp-Glu-Ser-Asn-Gly-Gln-Pro-Glu-Asn-Asn-Tyr. It is proposed that this is the typical sequence for residues 381–391 of human γ-chains.
Dorothy M. Parr, Theo Hofmann
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Chicken low molecular weight immunoglobulin heavy chains: A comparison with the gamma chain of man

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973
Abstract 1. 1. Peptide mapping and amino acid composition studies of the C-region of chicken low molecular weight (LMW) immunoglobulin heavy chains and of the gamma chain of human IgG were conducted. 2. 2. The data from the chicken heavy chain were compared with the data from the gamma chain of man in an attempt to correlate structural ...
Bob G. Sanders, James C. Travis, Kay L. Wiley   +2 more
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Monoclonal antibodies to subclass-specific antigenic determinants on equine immunoglobulin gamma chains and their characterization

Veterinary Immunology and Immunopathology, 1998
This paper describes the production of a panel of monoclonal antibodies (mAbs) identifying the four recognised equine IgG subisotypes IgG, IgGa, IgGb, IgGc and IgG(T). Pure preparations of the subisotypes for use in immunisations and testing were produced using a combination of gel filtration, salt precipitation, ion exchange chromatography and protein
Mark A. Holmes, D. Paul Lunn, Abhineet S. Sheoran   +2 more
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Detection in Normal Plasma of Immunoglobulin resembling the Protein of γ-Chain Disease

Nature, 1973
TUMOURS of the lymphoid system have from time to time presented protein products apparently unique to the neoplastic process, but found later to occur in inconspicuous amounts in the normal organism. Thus Bence Jones protein was described in the urine of a patient with multiple myeloma in 1848 (ref.
C. W. K. Lam, G. T. Stevenson
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Domains in immunoglobulins: Demonstration in human γ-chains

Immunochemistry, 1973
Abstract Human γ-chain was split by low concentrations of trypsin and the digests were analysed by SDS-PAS gel electrophoresis. A number of discrete bands appeared in time with apparent mol. wt of (in thousand) 43, 31, 25, 18, and 12, while the molecular weight of the γ-chain was 56,000 by this method.
H.G. Seijen, G. Koch, M. Gruber
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IMMUNOGLOBULIN GAMMA CHAINS OF A MONOTREME MAMMAL, THE ECHIDNA (TACHYGLOSSUS ACULEATUS): AMINO ACID COMPOSITION AND PARTIAL AMINO ACID SEQUENCE

International Journal of Immunogenetics, 1977
SUMMARYThe echidna represents the lowest stage in phytogeny at which molecules clearly homologous to IgG antibodies appear to occur. We provide evidence that a fraction of γ chains possess an unblocked N terminal sequence comparable to the VHIII sub‐group of human γ chains and that glycine is the C‐terminal residue. Statistical comparison of amino acid
J. L. Atwell, J. J. Marchalonis
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