Results 151 to 160 of about 51,044 (202)
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Fc and Fab Fragments from IgG2 Human Immunoglobulins Characterized
Nature New Biology, 1972Papain 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, 1989We 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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Fc-Like Fragments in Peptic Digests of Human Immunoglobulin G
The Journal of Immunology, 1968Summary When the products of digestion of human immunoglobulin G with pepsin are compared to those obtained with papain, one major difference appears to involve the recovery of the Fc fragment. An Fc-like fragment was isolated from peptic digests of a variety of human immunoglobulin G preparations, including 10 different samples obtained
R, Heimer, S H, Schnoll
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Immunoglobulin M: Fixation of Human Complement by the Fc Fragment
Science, 1972The 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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Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G
The Journal of Biochemistry, 1991We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent.
A, Zanma, Y, Matsumoto, Y, Masuho
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Fc Fragment of Immunoglobulin G in Normal Human Plasma and Urine
Nature, 1967IT 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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Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin
Nature, 1980Immunoglobulin (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.
R M, Parkhouse, J, Lifter, Y S, Choi
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Ultrastructure of the Fc fragment of human immunonoglobulin G
Immunochemistry, 1971Abstract 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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Structural Comparison of Fucosylated and Nonfucosylated Fc Fragments of Human Immunoglobulin G1
Journal of Molecular Biology, 2007Removal 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 ...
Shigeki, Matsumiya +8 more
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Characterization of the Fc′ Fragment of Immunoglobulin G in Normal Human Urine
Nature, 1969A 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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