Results 21 to 30 of about 50 (50)

Production and purification of Fab′ fragments from chicken egg yolk immunoglobulin Y (IgY)

Journal of Immunological Methods, 1993
Methods were described for the production of Fab and Fab' fragments from chicken egg yolk IgY also referred to as IgG by papain and pepsin digestion respectively. Pepsin digestion was found to be suitable for the large scale preparation and purification of Fab'.
E M, Akita, S, Nakai
openaire   +2 more sources

Crystal structure of human immunoglobulin fragment Fab new refined at 2.0 Å esolution

Proteins: Structure, Function, and Bioinformatics, 1992
AbstractThe three‐dimensional structure of the human immunoglobulin fragment Fab New (IgG1,λ) has been refined to a crystal‐lographic R‐factor of 16.9% to 2Å resolution. Rms deviations of the final model from ideal geometry are 0.014 Å for bond distances and 3.03° for bond angles.
F A, Saul, R J, Poljak
openaire   +2 more sources

De novo discovery of peptide-based affinity ligands for the fab fragment of human immunoglobulin G

Journal of Chromatography A, 2022
Antibody fragments and their engineered variants show true potential as next-generation therapeutics as they combine excellent targeting with superior biodistribution and blood clearance. Unlike full antibodies, however, antibody fragments do not yet have a standard platform purification process for large-scale production.
Xingqing Xiao, Ryan Kilgore, Sudeep Sarma, Wenning Chu, Stefano Menegatti, Carol K. Hall   +5 more
openaire   +2 more sources

Fab fragments imprinted SPR biosensor for real-time human immunoglobulin G detection

Biosensors and Bioelectronics, 2011
F(ab) fragments imprinted surface plasmon resonance (SPR) chip was prepared for the real-time detection of human immunoglobulin G (IgG). In order to attach polymerization precursor on SPR chip, the SPR chip surface was modified with allyl mercaptan. F(ab) fragments of the IgG molecules were prepared by papain digestion procedure and collected by fast ...
Ertürk, Gizem, Uzun, Lokman, Tümer, M. Aşkın, Say, Rıdvan, Denizli, Adil   +4 more
openaire   +2 more sources

Allotypic Determinants on the Fab Fragment of Rabbit Aa Locus Negative IgG-Immunoglobulin

The Journal of Immunology, 1971
Abstract Immunization of rabbits with a locus negative IgG immunoglobulin molecules obtained from an Aa2Aa2 rabbit suppressed in utero with anti-Aa2 resulted in isoantibodies directed against the a negative IgG molecules. The allotypic specificities are located on the Fab fragment of IgG and are absent on the Fc fragment. Peptide maps of
K L, Knight, A, Gilman-Sachs, R, Fields, S, Dray   +3 more
openaire   +2 more sources

Adsorptive stripping voltammetry of F(ab′)2and Fab fragments of anti-mouse immunoglobulin G

Journal of Pharmaceutical and Biomedical Analysis, 1989
The adsorptive stripping voltammetric behaviour of F(ab')2 and Fab fragments of anti-mouse immunoglobulin G is described. Conditions were optimized for the determination of these fragments with respect to accumulation potential, accumulation time, scan rate, pulse amplitude, drop size and electrolyte composition. The F(ab')2 and Fab fragments gave rise
E, Buckley, P, Reilly, J, Rodriguez Flores, R, O'Kennedy, M R, Smyth   +4 more
openaire   +2 more sources

Low‐Molecular‐Weight Antibody in Rabbit Urine: Identity with the Fab Immunoglobulin Fragment

Scandinavian Journal of Immunology, 1973
Urine rabbits immunized against and was analysed for a antibody content. Sixty to ninety percent of the hapten‐binding activity was, on gel chromatography. found to be eluted at the same position as Fab. No binding activity of lower molecular weight could be observed.
openaire   +3 more sources

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
openaire   +2 more sources

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 ...
Wayne F. Anderson, Amechand Boodhoo, Clifford D. Mol   +2 more
openaire   +1 more source

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
openaire   +2 more sources