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Genetic (Gm) Antigens associated with Subfragments from the Fc Fragment of Human Immunoglobulin G [PDF]
Nature, 1969 THE specific (γ) polypeptide chain of immunoglobulin G (IgG, ref. 1) molecules carries several genetic markers (Gm antigens)2,3 which can be detected by serological techniques. Each of the markers is associated with one of three subclasses of γ chain, called γ1, γ2 or γ3 chains4.
M. W. Turner +3 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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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
Unmesh Angre +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
Unmesh Angre +6 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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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.Oduro 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.Oduro Minta, R H Painter
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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.
Andrew G. Plaut +5 more
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Molecular Immunology, 1981
Abstract Papain-derived fragments (Fab and Fc) were used to localize previously uncharacterized chicken 7S immunoglobulin (Ig§) allotypic specificities (G-1.7, G-1.8, G-1.9, G-1.10, and G-1.12). Based on the molar amounts of Fab and Fc preparations relative to undigested 7S Ig to inhibit 50% of binding of 125 I-7S Ig with homologous alloantiserum ...
Lean Kuan Ch'ngi, Albert A. Benedict
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Abstract Papain-derived fragments (Fab and Fc) were used to localize previously uncharacterized chicken 7S immunoglobulin (Ig§) allotypic specificities (G-1.7, G-1.8, G-1.9, G-1.10, and G-1.12). Based on the molar amounts of Fab and Fc preparations relative to undigested 7S Ig to inhibit 50% of binding of 125 I-7S Ig with homologous alloantiserum ...
Lean Kuan Ch'ngi, Albert A. Benedict
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970
Abstract Sub-fragments of the Fc segment of normal human immunoglobulin G have been obtained by papain and pepsin hydrolysis. A comparative study of their physicochemical characteristics and biological activities has been conducted. Except for the Gm “1” allotypic marker, the pepsin sub-fragment, with a molecular weight of half that of Fc, retained ...
R. Hong, D. Frommel
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Abstract Sub-fragments of the Fc segment of normal human immunoglobulin G have been obtained by papain and pepsin hydrolysis. A comparative study of their physicochemical characteristics and biological activities has been conducted. Except for the Gm “1” allotypic marker, the pepsin sub-fragment, with a molecular weight of half that of Fc, retained ...
R. Hong, D. Frommel
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Research in Veterinary Science, 1976
The selective transport of blood IgG1 into colostrum in ruminant species is not well understood. Therefore, the transport of Fc fragments isolated from serum IgG1 (Fc gamma 1) and IgG2 (Fc gamma 2) in normal and pregnant goats was studied. The animals were injected intravenously with radio-labelled 125I-Fcgamma1 and 131I-Fcgamma2 fragments.
V.V. Micusan, A.G. Borduas
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The selective transport of blood IgG1 into colostrum in ruminant species is not well understood. Therefore, the transport of Fc fragments isolated from serum IgG1 (Fc gamma 1) and IgG2 (Fc gamma 2) in normal and pregnant goats was studied. The animals were injected intravenously with radio-labelled 125I-Fcgamma1 and 131I-Fcgamma2 fragments.
V.V. Micusan, A.G. Borduas
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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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