Results 341 to 350 of about 25,748,471 (370)

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

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.
X, Chu, Z H, Lin, G L, Shen, R Q, Yu
openaire   +2 more sources

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.
M A, Wiemers, N D, Stallman
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Primary Selective Deficiency of Immunoglobulin M

Internal Medicine Journal, 1978
Summary: Selective deficiency of IgM as a primary disorder is seldom encountered1–3, and the syndrome remains ill‐defined. It is generally accepted that for a diagnosis to be made, the serum IgM level should be consistently below 2 SD of normal, no other immunodeficiencies are present, and it is not secondary to other disease processes. This report of
Y H, Thong, G M, Maxwell
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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
R E, Cathou, D A, Holowka
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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 ...
openaire   +1 more source

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.
openaire   +2 more sources

Adsorptive voltammetric behaviour of immunoglobulin M

Talanta, 1991
The adsorptive voltammetric behaviour of immunoglobulin M (IgM) has been investigated at the static mercury drop electrode. The stripping process yields an analytically useful signal and the detection limit is 1.2 x 10(-10)M. The adsorptive voltammetric behaviour of IgM has been compared with that of IgG and streptavidin.
J M, Fernandez Alvarez, M R, Smyth, R, O'Kennedy   +2 more
openaire   +2 more sources

Post-rituximab immunoglobulin M (IgM) hypogammaglobulinemia.

Autoimmunity Reviews, 2020
K. Kridin, Abdul Razzaq Ahmed
semanticscholar   +1 more source

A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin μ chain gene

Nature, 1991
D. Kitamura, J. Roes, Ralf Kühn, K. Rajewsky   +3 more
semanticscholar   +1 more source