Results 261 to 270 of about 732,598 (320)

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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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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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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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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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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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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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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Effective treatment of experimental autoimmune neuritis with Fc fragment of human immunoglobulin

Journal of Neuroimmunology, 2007
IV immunoglobulin (IVIg) and its Fc fragment proved effective in preventing further progression of experimental autoimmune neuritis (EAN) in the rat induced by whole bovine peripheral nerve myelin and shortening disease duration. This effectiveness was associated with significant differences in electrophysiological parameters including less ...
Hsin Hsin, Lin, Min Xia, Wang, Judith M, Spies, John D, Pollard   +3 more
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Human Immunoglobulin A: Production of an Fc Fragment by an Enteric Microbial Proteolytic Enzyme

The Journal of Immunology, 1973
Summary An Fc fragment has been prepared in good yield by proteolytic cleavage of human secretory and serum myeloma IgA with an enzyme recovered from the human gastrointestinal tract. The naturally occurring enzyme is of microbial origin and its activity is metal dependent.
S K, Mehta, A G, Plaut, N J, Calvanico, T B, Tomasi   +3 more
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Regulation of the immune response: III. The role of macrophages in the potentiation of the immune response by Fc fragments.

Journal of Immunology, 1981
The Fc fragment-induced enhancement of the anti-SRBC response was found to be dependent upon the presence of functional macrophages. Fc fragments derived from human immunoglobulin were unable to enhance either the in vivo or in vitro anti-SRBC response ...
E. Morgan, W. Weigle
semanticscholar   +1 more source