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Structural insights into immunoglobulin M

Science, 2020
Hefty structures of IgA and IgM complexes Immunoglobulin M (IgM) and IgA are antibody isotypes that can form higher-order secretory complexes (sIgM and sIgA), which allows them to effectively bind and neutralize antigens with low-affinity repetitive epitopes, such as those found on the surface of many bacteria and viruses.
Yaxin Li   +11 more
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Immunoglobulin M mutants

European Journal of Immunology, 1980
AbstractMutants of a hybridoma line secreting IgM with anti‐trinitrophenyl specificity were enriched by coupling the hapten to the cell surface and incubating the cells in the presence of complement. In this way, cells secreting wild‐type Ig commit suicide, whereas cells secreting IgM with reduced lytic activity preferentially survive.
Georges Köhler, Marc J. Shulman
openaire   +1 more source

Pregnancy in immunoglobulin M nephropathy

Journal of Obstetrics and Gynaecology Research, 2017
AbstractImmunoglobulin M nephropathy is an uncommon glomerular disease and a relatively less recognized clinico‐immunopathological entity in the domain of glomerulonephritis, often thought to be a bridge between minimal change disease and focal segmental glomerulosclerosis.
Meryem, Hocaoğlu   +3 more
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Post-rituximab immunoglobulin M (IgM) hypogammaglobulinemia

Autoimmunity Reviews, 2020
Rituximab is a B cell depleting monoclonal antibody that targets the B cell-specific cell surface antigen CD20 and is currently used to treat several autoimmune diseases. The elimination of mature CD20-positive B lymphocytes committed to differentiate into autoantibody-producing plasma cells is considered to be the major effect of rituximab, that makes
Khalaf, Kridin, A Razzaque, Ahmed
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Polymerization of human immunoglobulin M

Biochemistry, 1978
The repolymerization of human IgM following mild reductive cleavage was studied as a model for intracellular polymer assembly. Repolymerization was found to require the presence of J chain and a disulfide exchanging system which could be furnished either intrinsically by the use of the monofunctional thiol mercaptoethylamine or extrinsically by the ...
C E, Wilde, M E, Koshland
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Immunoglobulin G paraprotein cross-reactivity with immunoglobulin M measurement

Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 2008
We report a case of IgG paraprotein cross-reactivity with IgM measurement in a patient with IgGκ multiple myeloma and associated IgA and IgM immune paresis. IgM measurements using a Beckman-Coulter Synchron LX IgM reagent initially gave unmeasurably low IgM concentrations (<0.3 g/L) but IgM quantitation using later batches of reagent gave IgM ...
Robert C, Hawkins, Lian-King, Lee
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Purification of Immunoglobulin M and Immunoglobulin D

Current Protocols in Immunology, 1997
AbstractThis unit describes two classical protocols for the purification of IgM ‐ dialysis of ascites fluid, tissue culture medium, or bioreactor supernatants against distilled water to precipitate pure IgM, and ammonium sulfate precipitation. Both protocols can be followed by size‐exclusion chromatography to obtain a highly purified product.
S M, Andrew   +3 more
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Human immunoglobulin M stimulates adipocyte lipogenesis

Metabolism, 1984
In view of our recent demonstration that human immunoglobulin G (IgG) and its Fc moiety exert a stimulatory effect on lipogenesis by adipocytes, we have examined the possibility that human immunoglobulin M (IgM) may induce a similar effect upon adipocytes.
M A, Khokher, R J, Woods, P, Dandona
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Selective Immunoglobulin M Deficiency in Foals

Journal of the American Veterinary Medical Association, 1977
SUMMARY Selective immunoglobulin M deficiency was diagnosed in 5 foals, on the basis of reduced serum immunoglobulin M concentrations (more than 2 standard deviations below the normal mean). All 5 foals had clinical signs or lesions involving the respiratory tract.
L E, Perryman   +2 more
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Structural studies on bovine immunoglobulin M

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972
Abstract Heavy (μ) and light polypeptide chains were prepared from normal bovine IgM and were found to have molecular weights of 61 800 and 22 800. Heavy chain from a human pathological IgM had a molecular weight of 65 200. Bovine μ-chain contained 12% carbohydrate but the light chain contained less than 0.5%. The human μ-chain was found to have 15%
D, Beale, N, Buttress
openaire   +2 more sources

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