Results 221 to 230 of about 22,044 (247)

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-
Ingemar Berggård, Hans Bennich
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Isolation of Fab and Fc fragments from mouse immunoglobulin Gl

Bulletin of Experimental Biology and Medicine, 1979
Two methods of isolating Fab- and Fc-fragments from mouse immunoglobulin G1 are presented. The first method involves fractionation of papain protein hydrolysate on a column with DEAE- (or DE-32)-cellulose adjusted with 0.005 M K-phosphate buffer, pH 8. The Fab-fragment was eluted from the column with the starting buffer.
B V Nikonenko, E V Sidorova, E L Beliaeva   +2 more
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Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin

Nature, 1980
Immunoglobulin (Ig) molecules of the M and D classes are present on the membranes of B lymphocytes (sIg), where they serve as antigen receptors1–6. sIg is a biosynthetically stable membrane protein which requires either denaturing conditions or detergents to free it from other membrane constituents1,7–9.
John Lifter, Yong Sung Choi, R. M. E. Parkhouse   +2 more
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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.
H. Hugh Fudenberg, An-Chuan Wang
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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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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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NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein

Biomolecular NMR Assignments, 2021
The Fc portion of immunoglobulin G (IgG) promotes defensive effector functions in the immune system by interacting with Fcγ receptors and complement component C1q. These interactions critically depend on N-glycosylation at Asn297 of each CH2 domain, where biantennary complex-type oligosaccharides contain microheterogeneities resulting primarily from ...
Yoshiki Yamaguchi, Ichio Shimada, Koichi Kato, Koichi Kato, Rina Yogo, Rina Yogo, Takeshi Takizawa, Saeko Yanaka, Saeko Yanaka, Yohei Miyanoiri   +9 more
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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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Structural Comparison of Fucosylated and Nonfucosylated Fc Fragments of Human Immunoglobulin G1

Journal of Molecular Biology, 2007
Removal of the fucose residue from the oligosaccharides attached to Asn297 of human immunoglobulin G1 (IgG1) results in a significant enhancement of antibody-dependent cellular cytotoxicity (ADCC) via improved IgG1 binding to Fcgamma receptor IIIa. To provide structural insight into the mechanisms of affinity enhancement, we determined the crystal ...
Mayumi Nagano, Yoshiki Yamaguchi, Hiroaki Sasakawa, Mitsuo Satoh, Koichi Kato, Koichi Kato, Jun-ichi Saito, Kenya Shitara, Shizuo Otaki, Shigeki Matsumiya   +9 more
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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 C epsilon 3 domain responsible for binding to alpha chain of high affinity Fc receptor for IgE (Fc epsilon RI alpha), but it remains unknown for the enzyme susceptibility.
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