Results 191 to 200 of about 49,117 (237)

The Alternative Binding Site for Protein A in the Fab Fragment of Immunoglobulins

Scandinavian Journal of Immunology, 1993
Twenty‐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.
S, Ibrahim, M, Kaartinen, I, Seppälä, A, Matoso-Ferreira, O, Mäkelä   +4 more
openaire   +2 more sources

Use of molecular replacement in the solution of an immunoglobulin Fab fragment structure

Acta Crystallographica Section B Structural Science, 1991
Molecular-replacement efficiency depends highly on structural and sequence homologies between available models and the molecule in the crystal being studied. The structure of the Fab fragment of an antibody specific for an influenza virus hemagglutinin was determined by molecular replacement and the Fv and the CH1:CL parts were localized separately ...
T, Bizebard, Y, Mauguen, J J, Skehel, M, Knossow   +3 more
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

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

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

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

Dissociation and denaturation equilibriums and kinetics of a homogeneous human immunoglobulin Fab fragment

Biochemistry, 1976
The conformational equilibria and the kinetics of the approach to equilibrium of an IgG1 myeloma (Wes) Fab fragment (SSFab) and its mildly reduced and S-carboxyamidomethylated derivative (RAFab) were studied as a function of guanidine hydrochloride concentration.
openaire   +2 more sources

Structure of chicken 7S immunoglobulin allotypes: Further studies on localization to Fab and Fc fragments

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 ...
L K, Ch'ng, A A, Benedict
openaire   +2 more sources

[Isolation of FAB and Fc fragments from murine immunoglobulin G1].

Biulleten' eksperimental'noi biologii i meditsiny, 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.
E L, Beliaeva, B V, Nikonenko, E V, Sidorova   +2 more
openaire   +1 more source