Results 261 to 270 of about 45,837 (320)

Immunoglobulin M: Fixation of Human Complement by the Fc Fragment

Science, 1972
The Fc fragment [(Fc) 5 μ, with a molecular weight of 342,000] of human immunoglobulin M from patients with Waldenström's macroglobulinemia has a complement fixing ability approximately 19 times greater on a molar basis than that of the parent immunoglobulin M.
A G, Plaut, S, Cohen, T B, Tomasi
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Impairment by glycation of immunoglobulin G Fc fragment function

Scandinavian Journal of Clinical and Laboratory Investigation, 1990
Incubation of human immunoglobulin G (IgG) with glucose in vitro leads to the formation of glycated IgG concomitant with marked changes in functional properties of the Fc fragment. After 22 days of incubation in the absence and presence of 13.9, 27.7 and 55.5 mmol/l glucose, respectively, protein A binding was reduced by 42, 66 and 83%, depending on ...
R, Dolhofer-Bliesener, K D, Gerbitz
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Ultrastructure of the Fc fragment of human immunonoglobulin G

Immunochemistry, 1971
Abstract Crystals of the plasmin Fc fragment of human immunoglobulin G have been examined in the electron microscope at various stages during dissociation and recrystallization. Two characteristic shapes are recognized in the micrographs. One is a double, concentric annulus in which the outer annulus is seen to consist of 12 masses disposed radially ...
L, Pinteric, R H, Painter, G E, Connell
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Characterization of the Fc′ Fragment of Immunoglobulin G in Normal Human Urine

Nature, 1969
A FRAGMENT in normal human urine related specifically to the heavy chains of immunoglobulin G (IgG) was found1 by gel diffusion and immunoelectrophoretic analysis to be antigenically similar to the Fc′ fragment produced by papain digestion of the IgG molecule.
M W, Turner, I, Berggård
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Fc Fragment of Immunoglobulin G in Normal Human Plasma and Urine

Nature, 1967
IT has been shown that immunoglobulins of low molecular weight (micro-immunoglobulins) in normal human urine (compare ref. 1) are predominantly composed of material which closely resembles light polypeptide chains2. This is also true of the micro-immunoglobulins in “post-exercise” urine3 and in urine from patients with connective tissue disease4. Micro-
I, Berggård, H, Bennich
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Fc and Fab Fragments from IgG2 Human Immunoglobulins Characterized

Nature New Biology, 1972
Papain digestion of 7S immunoglobulin G (IgG) produces two 3.5S Fab fragments and one 3.5S Fc fragment1–8. The Fab fragment contains one light chain and one Fd fragment and is still able to combine specifically univalently with antigen. The Fc fragment is a dimer of the carboxyl terminal half of the heavy chain.
A C, Wang, H H, Fudenberg
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IgC Fc fragments induce B cell differentiation and immunoglobulin secretion

Immunology Letters, 1989
We now show that the Fc fragment is capable of inducing B cell differentiation and secretion of immunoglobulins (Igs) in human mononuclear cells from peripheral blood (PBMC). The absolute number of plasma cells observed in all individuals tested is similar.
E D, Carosella, J, Armand
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Interference with tolerance induction of primed B cells by the Fc fragment of immunoglobulin

Cellular Immunology, 1984
The capacity to interfere with tolerance induction in primed B cells was examined. Previous work had shown that TNP-specific splenic B cells from mice primed and boosted with TNP-KLH are highly susceptible to in vitro tolerization upon a brief exposure to TNP on a carrier unrelated to KLH.
Walker, S M, Fraker, P J, Weigle, W O
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Unsusceptibility of recombinant human Fc fragments of immunoglobulin E to thrombin

Human Antibodies, 1996
Human immunoglobulin E (IgE) contains a potential recognition sequence for thrombin protease cleavage at N-terminal end of Cε3 domain responsible for binding to α chain of high affinity Fc receptor for IgE (FcεRICα, but it remains unknown for the enzyme susceptibility.
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Preliminary crystallographic study of the Fc fragment of a monoclonal IgG2b murine immunoglobulin

Journal of Molecular Biology, 1983
The Fe fragment of a gamma 2b murine monoclonal anti-p-azophenylarsonate antibody (R19.9, IgG2b, kappa) has been crystallized. The crystals are tetragonal, space group P41 (or P43) with unit cell dimensions: a = b = 134.3 +/- 1.1 A, c = 144.0 +/- 0.7 A.
Comarmond, M, Tougard, P
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