Results 321 to 330 of about 585,196 (339)
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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
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Piezoelectric immunosensor for the detection of immunoglobulin M

The Analyst, 1995
A piezoelectric immunosensor has been developed for the determination of human IgM. The crystals are AT-cut and have a basic resonant frequency of 9 MHz. Immobilization of goat antihuman IgM antibodies to the crystals' surfaces was accomplished via a CNBr-activated copolymer coating of 2-hydroxyethyl methacrylate and methylmethacrylate.
Zhao-Hui Lin   +3 more
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Immunoglobulin M in murray valley encephalitis

Pathology, 1975
Twelve clinical cases of Murray Valley encephalitis are described, in which the sero-diagnosis was confirmed by the detection of Murray Valley encephalitis immunoglobulin M.
Neville D. Stallman, Margaret A. Wiemers
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Process‐Scale Purification of Immunoglobulin M Concentrate [PDF]

open access: possibleVox Sanguinis, 1993
AbstractAn IgM concentrate was purified from Cohn fraction III. Efficiency of euglobin precipitation was shown to be controlled by pH and ionic strength. Prekallikrein activator activity in the product was insignificant. Overall yield from the octanoic acid supernate and purity of the concentrate were 66 ± 8 (n = 16) and 50 ± 5% (n = 16), respectively.
Grace C. Tsay   +4 more
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Immunochemical studies of an immunoglobulin M-immunoglobulin G mixed cryoglobulin

Clinical Immunology and Immunopathology, 1978
Abstract A mixed IgG-IgM cryoglobulin was isolated from a patient with arthritis and glomerulonephritis. Electron microscopic examination of both cryoprecipitate and glomerular deposits revealed unusual structures designated as “cylindrical and annular bodies.” The IgM component was monoclonal and had antibody activity against IgG molecules ...
A. C. Wang   +2 more
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Evolution of Conformational Flexibility of Immunoglobulin M

1975
Since the initial observations of Heidelberger and Pederson (1) of a macroglobulin antibody against pneumococcus in the horse, IgM has been recognized as a major class of immunoglobulins in mammals as well as in vertebrates as phylogenetically distant as the elasmobranchii (2). In fact, IgM appears to be the first recognizable class to have evolved. It
Renata E. Cathou, David A. Holowka
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Characteristics of immunoglobulin A nephropathy with mesangial immunoglobulin G and immunoglobulin M deposition

Nephrology, 2010
There are immunoglobulin (Ig)A nephropathy (IgAN) cases showing mesangial IgG and/or IgM deposition, however, their characteristics have remained unknown.Three hundred and eighty-four IgAN patients were divided according to the existence of mesangial IgG and/or IgM deposition: IgA deposition only (A group, n = 77); IgA and IgM deposition (AM group, n = 
Ari Shimizu   +5 more
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Neutralization by Immunoglobulin M

1993
The pentameric nature of IgM ensures high avidity (about 107-fold greater than Fab) for structures bearing repeated identical antigenic determinants, but in general IgM is of low specificity since its variable region genes are not subject to hypermutation modification that occurs in cells synthesizing IgG or IgA and increases the affinity of these ...
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An allotypic marker on chicken immunoglobulin M

European Journal of Immunology, 1974
AbstractAn allotypic marker, present on IgM, but not IgG, molecules in sera from chickens of the inbred CA, CB and G‐B1 lines, is described. The marker, called “C‐Ml”, is absent in sera from birds of the WA and WB lines, and its segregation in (CB × WA)F2 birds is consistent with its inheritance as a single dominant factor.
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Isolation of Murine and Human Immunoglobulin M and Murine Immunoglobulin D

Current Protocols in Immunology, 2009
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.
Ashok Amin   +3 more
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