Results 271 to 280 of about 45,837 (320)
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Effective treatment of experimental autoimmune neuritis with Fc fragment of human immunoglobulin
Journal of Neuroimmunology, 2007IV 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 +3 more
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NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein
Biomolecular NMR Assignments, 2021The 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 ...
Saeko Yanaka +6 more
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Human Immunoglobulin A: Production of an Fc Fragment by an Enteric Microbial Proteolytic Enzyme
The Journal of Immunology, 1973Summary 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 +3 more
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Expression of Fc Fragment Receptors of Immunoglobulin G (Fc?Rs) in Rat Hepatic Stellate Cells
Digestive Diseases and Sciences, 2005Hepatic stellate cells (HSCs) are now considered the major cell type in the liver mediating the development of liver fibrosis. Recently it was demonstrated that HSCs express membrane proteins involved in antigen presentation. We further evaluate immunological properties of HSCs by examining the expression and function of the Fc fragment of ...
Hong, Shen +5 more
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Journal of Chromatography B, 2020
We describe a simplified approach for purification and characterization of human 'IgG-Fc' fragment used widely as immunochemical tool and for therapeutic purposes. The 'Fc' fragment was purified from human IgG in a 3-stage column chromatography. The purified 'Fc' fragment appeared as a dimer glycoprotein with an apparent molecular mass of 52,981 Dalton
Jatin B, Tandale +6 more
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We describe a simplified approach for purification and characterization of human 'IgG-Fc' fragment used widely as immunochemical tool and for therapeutic purposes. The 'Fc' fragment was purified from human IgG in a 3-stage column chromatography. The purified 'Fc' fragment appeared as a dimer glycoprotein with an apparent molecular mass of 52,981 Dalton
Jatin B, Tandale +6 more
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Immunochemistry, 1972
Abstract The major electrophoretic components of Fc prepared by plasmin digestion of human IgG ( γ 1 subclass) have been isolated and their physical, chemical and biological properties examined. The individual components showed the same amino acid composition, the same amino terminal residue, threonine, and were shown to have the same sedimentation
J O, Minta, R H, Painter
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Abstract The major electrophoretic components of Fc prepared by plasmin digestion of human IgG ( γ 1 subclass) have been isolated and their physical, chemical and biological properties examined. The individual components showed the same amino acid composition, the same amino terminal residue, threonine, and were shown to have the same sedimentation
J O, Minta, R H, Painter
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An easy and simple separation method for Fc and Fab fragments from chicken immunoglobulin Y (IgY).
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2020Xin Zhou, Yanru Wang, D. Ahn, Z. Cai
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Production of an Fc Fragment from Human Immunoglobulin a by an IgA-Specific Bacterial Protease
1974Enzymatic proteolysis of human immunoglobulin A yields Fabα fragments but the Fcα is degraded to small peptides. The unavailability of Fcα has hampered to some extent certain studies of IgA, e.g., its primary structure and the attachment site of secretory component and J chain.
A G, Plaut, R J, Genco, T B, Tomasi
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The binding of protein A of immunoglobulin G and of Fab and Fc fragments.
Acta pathologica et microbiologica Scandinavica. Section C, Immunology, 1979Results are presented to show that protein A (pA) may fix to the Fab region of IgG outside the antigen binding site. Thus, pA-reactive Fab fragments were isolated both from specific anti-egg albumin and specific anti-measles virus antibodies. A probable significance of this Fab reactivity in the precipitation reaction between IgG and pA is discussed ...
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Zeitschrift für Immunitätsforschung: Immunobiology, 1978
Molecular weight determinations of immunoglobulin D suggest the presence of an extra region of the delta chain. In an attempt to locate this region, an IgDlambda myeloma protein (Gur), was digested with trypsin for 4 min at 56 degrees and the Fc fragment isolated by ion exchange chromatography.
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Molecular weight determinations of immunoglobulin D suggest the presence of an extra region of the delta chain. In an attempt to locate this region, an IgDlambda myeloma protein (Gur), was digested with trypsin for 4 min at 56 degrees and the Fc fragment isolated by ion exchange chromatography.
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