Results 151 to 160 of about 45,350 (212)

Investigation of the cooperative structure of Fc fragments from myeloma immunoglobulin G.

Biochemistry, 1998
The cooperative structure of Fc fragments prepared from myeloma human IgG1 was studied using scanning microcalorimetry and fluorescence at pH 4.2-8.0. It was shown that the first to be melted are CH2 domains whose interaction with each other is rather weak, while that with CH3 domains is strong.
V. Tischenko, V. Abramov, V. Zav'yalov
semanticscholar   +4 more sources

Denaturation by guanidine hydrochloride of the Fc(t) and pFc' fragments of human immunoglobulin G.

The Journal of Biochemistry, 1982
The denaturation and renaturation by guanidine hydrochloride of Fc(t) fragment whose interchain disulfide bonds are reduced and alkylated (R.A.Fc(t)) and pFc' fragment of a human myeloma protein (IgGl, kappa) were studied using tryptophyl fluorescence. R.A.Fc(t) was found to consist of a slow-unfolding region and a rapid-unfolding region.
A. Sumi, K. Hamaguchi
semanticscholar   +4 more sources

Identity of the Fc fragments of pathological and normal human immunoglobulin M.

Biochemistry, 1974
G. Florent, D. Lehman, D. Lockhart, F. Putnam   +3 more
semanticscholar   +4 more sources

Immunoglobulin M: Fixation of Human Complement by the Fc Fragment [PDF]

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.
Stanley Cohen, Thomas B. Tomasi, Andrew G. Plaut   +2 more
openaire   +2 more sources

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.
Akira Zanma, Yasuhiko Masuho, Yoh-Ichi Matsumoto   +2 more
openaire   +3 more sources

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 ...
K D Gerbitz, R Dolhofer-Bliesener
openaire   +3 more sources

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.
Ingemar Berggård, M. W. Turner
openaire   +3 more sources

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
openaire   +3 more sources

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
openaire   +3 more sources

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
openaire   +3 more sources