Results 161 to 170 of about 24,729 (207)
Expression of Antibody Fab Fragments and Whole Immunoglobulin in Mammalian Cells
Pietro Paolo Sanna
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The Alternative Binding Site for Protein A in the Fab Fragment of Immunoglobulins
Scandinavian Journal of Immunology, 1993Twenty‐six new human or murine monoclonal immunoglobulins (IgM, IgA, murine IgGl or human IgG3) with a known V‐region sequence were tested for alternative (non‐Fc) binding to Staphylococcal protein A. Seven of them did not bind at all. Four immunoglobulins (all mouse IgGl) were bound but easily eluted (at pH 6). They were probably bound via the Fc part.
Matti Kaartinen+4 more
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Allotypic markers on Fab fragments of mouse immunoglobulins.
Journal of immunology (Baltimore, Md. : 1950), 1974Abstract Allotypic determinants were detected on the Fab fragments of mouse IgG by guinea pig antisera prepared against polymerized Fab fragments of IgG from the C57BL and AKR strains. Different markers were detected by the two antisera. Indirect precipitation, with 125I-labeled Fab as ligand, was used for the assay.
Spring, S B, Nisonoff, A
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Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin
Nature, 1980Immunoglobulin (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.
John Lifter+2 more
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An EM study of phosphorylcholine-binding Fab′ immunoglobulin fragment crystals
Journal of Ultrastructure Research, 1975The Fab′ fragment of McPC603 mouse myeloma immunoglobulin with phosphorylcholine-binding activity crystallizes into both a hexagonal and a cubic structure. Models of these structures showing approximate molecular packing were deduced from an electron microscopic examination of stained crystal sections, a preliminary X-ray diffraction study, and the ...
David M. Segal+3 more
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Isolation of Fab and Fc fragments from mouse immunoglobulin Gl
Bulletin of Experimental Biology and Medicine, 1979Two 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+2 more
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Immunoglobulin Fab fragment-binding proteins
International Journal of Immunopharmacology, 1994Five molecules are known to bind the Fab fragments of human immunoglobulins (Ig). Microbial protein A and protein G are primarily Fc-binding molecules but can also bind other structures of the heavy chain, which are located in the variable domain of the third subgroup (VH3) and in the first constant domain of IgG (CH1 gamma), respectively. In contrast,
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Fc and Fab Fragments from IgG2 Human Immunoglobulins Characterized
Nature New Biology, 1972Papain 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
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Journal of Chromatography A, 2005
The development and characterization of an artificial protein L (PpL) for the affinity purification of antibodies is described. Ligand 8/7, which emerged as the lead from a de novo designed combinatorial library of ligands, inhibits the interaction of PpL with IgG and Fab by competitive ELISA and shows negligible binding to Fc. The ligand 8/7 adsorbent
A. Cecília A. Roque+2 more
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The development and characterization of an artificial protein L (PpL) for the affinity purification of antibodies is described. Ligand 8/7, which emerged as the lead from a de novo designed combinatorial library of ligands, inhibits the interaction of PpL with IgG and Fab by competitive ELISA and shows negligible binding to Fc. The ligand 8/7 adsorbent
A. Cecília A. Roque+2 more
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The importance of purity in the crystallization of DNA binding immunoglobulin Fab fragments
Journal of Crystal Growth, 1988Abstract As part of a program to determine the structures of a number of immunoglobulin F ab fragments that are specific for different DNA structures or sequences, the affects of sample purity upon crystallization have been studied. The protease treatment utilized to produce F ab fragments introduces micro-heterogeneity into the sample which is ...
Amechand Boodhoo+2 more
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