Results 211 to 220 of about 57,044 (253)

Tokenizing loops of antibodies. [PDF]

MAbs
Fang A, Alberstein RG, Kelow S, Dreyer FA.   +3 more
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Alpha-Chain Disease: A New Immunoglobulin Abnormality

Science, 1968
A new type of pathological immunoglobulin was found in the serum, urine, and saliva of a young Arab patient with abdominal lymphoma and diffuse lymphoplasmacytic infiltration of the small intestine. This protein is devoid of light chains and is closely related to the alpha polypeptide chains of the γ A1 (Le ...
M, Seligmann, F, Danon, D, Hurez, E, Mihaesco, J L, Preud'homme   +4 more
openaire   +4 more sources

Variant of a human immunoglobulin: “Alpha chain disease” protein AIT

Biochemical and Biophysical Research Communications, 1975
Summary Protein AIT is a human alpha chain disease protein belonging to the IgAl subclass. It has a molecular weight of 34,200 instead of 55,000 for intact a chain. It contains an internal deletion which comprises about the entire Fd fragment. Normal synthesis resumes at a valine residue in the middle of the heavy chain where a series of short ...
C, Wolfenstein-Todel, E, Mihaesco, B, Frangione   +2 more
openaire   +2 more sources

Gene segments encoding membrane domains of the human immunoglobulin gamma 3 and alpha chains

Immunogenetics, 1990
The carboxyterminal region of the heavy chains, according to its hydrophilic or hydrophobic properties, determines whether the immunoglobulin will be secreted or membrane-bound. We have determined the nucleotide sequences of the human IGHG3, IGHA1, and IGHA2 membrane exons isolated from genomic DNA libraries.
Bensmana, M, Lefranc, M.P.
openaire   +2 more sources

Alpha Chain Determinants on the Membrane of Immunoglobulin Synthesizing Cells

1974
In a study of surface immunoglobulins (Ig) on lymphocytes from patients with paraproteinemia (1), we observed that a variable number of plasma cells not only contained intracellular Ig, but also had Ig on their surface, as shown in the vital technique of immunofluorescence.
Hijmans, W., Schuit, H.R.E., Radl, J., Vossen, J.M.J.J.   +3 more
openaire   +3 more sources

Evolutionary Relationship between Carboxyterminal Region of a Human Alpha Chain and Other Immunoglobulin Heavy Chain Constant Regions

Nature, 1973
FROM an evolutionary point of view the earliest immunoglobulins to appear are widely considered to be members of the IgM class, primarily because of their presence in many lower phylogenetic forms1. The IgG class is believed to be of more recent origin.
C Y, Chuang, J D, Capra, J M, Kehoe
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Alpha chain of HLA-DR transplantation antigens is a member of the same protein superfamily as the immunoglobulins

Cell, 1982
Four cDNA clones, pDR-alpha-1, pDR-alpha-2, pDR-alpha-3 and pDR-alpha-4, corresponding to the alpha chain of HLA-DR antigens, have been sequenced. Restriction maps and sequences suggest that all clones are identical apart from a single-base substitution present in pDR-alpha-1.
D, Larhammar, K, Gustafsson, L, Claesson, P, Bill, K, Wiman, L, Schenning, J, Sundelin, E, Widmark, P A, Peterson, L, Rask   +9 more
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Allotypes of rat immunoglobulins—II. Distribution of the allotypes of kappa and alpha chain loci in different inbred strains of rats

Immunochemistry, 1974
Abstract Two allotypic markers, termed Iκ (1a) and Iκ (1b), were detected on rat kappa light chains fromthe LOU/C/Wsl and OKAMOTO strains of rats respectively. This allotypic specificity is not linked to a previously described alpha-chain allotypic locus.
A, Beckers, P, Querinjean, H, Bazin
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Immunoglobulin-like nature of the α-chain of a human T-cell antigen/MHC receptor

Nature, 1984
Although the receptor with which T cells bind specific antigen can, like immunoglobulin, distinguish between antigens which differ only slightly in structure, it is unique in recognizing antigen only in conjunction with one of the self proteins of the major histocompatibility complex (MHC restriction).
C H, Hannum, J W, Kappler, I S, Trowbridge, P, Marrack, J H, Freed   +4 more
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Characterization of a disulfide bridge linking the J chain to the α chain of polymeric immunoglobulin A

Biochemical and Biophysical Research Communications, 1973
Summary The “J chain” has been shown to be an integral part of polymeric IgA and IgM molecules and to be disulfide bridged. Diagonal electrophoresis has localized a disulfide bridge to the cysteine in the carboxy terminal peptide: Ala-Glu-Val-Asp-Gly-Thr-Cys-Tyr of the α chain and the J chain peptide Ala-Cys-Arg.
E, Mendez, F, Prelli, B, Frangione, E C, Franklin   +3 more
openaire   +2 more sources