Results 171 to 180 of about 45,350 (212)
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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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FC-like fragments in peptic digests of human immunoglobulin G.
Journal of Immunology, 1968When 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.
R. Heimer, S. Schnoll
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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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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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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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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract The effect of alkyl sulfates of various chain lengths on immunoglobulin fragment Fc(t) was studied. Circular dichroism measurements indicated that the non-helical polypeptide chains of Fc(t) were ordered by anionic detergents to a certain degree.
Pak Kai Jane Lee, Bruno Jirgensons
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Abstract The effect of alkyl sulfates of various chain lengths on immunoglobulin fragment Fc(t) was studied. Circular dichroism measurements indicated that the non-helical polypeptide chains of Fc(t) were ordered by anionic detergents to a certain degree.
Pak Kai Jane Lee, Bruno Jirgensons
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