Results 161 to 170 of about 24,709 (211)

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
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Immunoglobulin Fab fragment-binding proteins

International Journal of Immunopharmacology, 1994
Five 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, 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
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An artificial protein L for the purification of immunoglobulins and Fab fragments by affinity chromatography

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, M Angela Taipa, Christopher R. Lowe   +2 more
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The importance of purity in the crystallization of DNA binding immunoglobulin Fab fragments

Journal of Crystal Growth, 1988
Abstract 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, Clifford D. Mol, Wayne F. Anderson   +2 more
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Bacterial Proteins and Their Proposed Interactions with Fc or Fab Fragments of Immunoglobulins

Biochemistry & Physiology: Open Access, 2014
The reactivity of Immunoglobulin Binding Proteins (IBP) to Fc and/or Fab fragments of immunoglobulins was summarized in this review. Staphylococcal protein A (SpA), Streptococcal protein G and Peptostreptococcal protein L (SpL) were the IBP reported. SpA reacted with IgG from skunk, coyote, raccoon, mule and donkey.
Sehlule Vuma, Wayne Mohammed, Angel A. Justiz Vaillant   +2 more
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Binding of rabbit immunoglobulin G Fab fragments to subtilisin Carlsberg

Molecular Immunology, 1973
Abstract The interaction of crystalline subtilisn Carlsberg with pooled rabbit anti-subtilisin serum was studied by classical precipitin reaction techniques. In addition, Fab fragments were obtained from the rabbit immunoglobulins precipitated by subtilisin, and the interaction between Fab fragments and antigen was studied in the analytical ...
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Disposition of a monoclonal anti-phencyclidine Fab fragment of immunoglobulin G in rats.

The Journal of Pharmacology and Experimental Therapeutics, 1993
Treatment of drug toxicity is problematic for compounds like phencyclidine (PCP) which have no known antagonists. With the advent of technology for production of large amounts of monoclonal antibody, it is now possible to explore the use of these antibodies as high affinity in vivo antagonists for treatment of PCP overdose.
M B, McClurkan, J L, Valentine, L, Arnold, S M, Owens   +3 more
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Design and analysis of PCR primers for the amplification and cloning of human immunoglobulin Fab fragments

Human Antibodies, 1994
We have developed PCR primers for the amplification and cloning of the genes encoding human antibody fragments. Two sets of primers were designed to amplify the coding sequence of the complete variable region and the first constant domain of immunoglobulin heavy chains.
S Y Chang, G Eichinger, M de Boer, H C Wong   +3 more
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Positive response to surfactants on the interfacial behavior and aggregation stability of Fab fragments from yolk immunoglobulin

International Journal of Biological Macromolecules, 2021
The antigen binding fragment (Fab) is pepsin-digested product from egg yolk immunoglobulin (IgY), which shows lower immunogenicity and higher antibacterial activity. However, it limited the application of Fab due to the spontaneous adsorption and aggregation at the air-liquid interface.
Zhaoxia Cai, Minquan Xia, Xin Zhou, Yanru Wang, Long Sheng   +4 more
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