Results 101 to 110 of about 24,903 (156)

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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Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G

The Journal of Biochemistry, 1991
We 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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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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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.
R M, Parkhouse, J, Lifter, Y S, Choi
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Fc-Like Fragments in Peptic Digests of Human Immunoglobulin G

The Journal of Immunology, 1968
Summary 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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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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