Results 11 to 20 of about 50 (50)

Allotypic Markers on Fab Fragments of Mouse Immunoglobulins

The Journal of Immunology, 1974
Abstract 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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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.
A C, Wang, H H, Fudenberg
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An EM study of phosphorylcholine-binding Fab′ immunoglobulin fragment crystals

Journal of Ultrastructure Research, 1975
The 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 ...
L W, Labaw, E A, Padlan, D M, Segal, D R, Davies   +3 more
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Crystallographic Data for the Fab Fragment of a Human Myeloma Immunoglobulin

Nature, 1968
COMPARISONS of the physical properties and chemical structure of myeloma proteins with those of other immunoglobulins and antibodies have indicated that myeloma proteins are abnormal only in their relative homogeneity; they seem to be typical representatives of the immunoglobulin class to which they belong. In addition, antibody activity has been shown
AVEY H. P, POLJAK R. J, ROSSI, GUIDO, NISONOFF A.   +3 more
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Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin

Nature, 1980
Immunoglobulin (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.
R M, Parkhouse, J, Lifter, Y S, Choi
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Competent Antigen-Binding Fragments (Fab) from Secretory Immunoglobulin A Using Streptococcus sanguis Immunoglobulin A Protease

Caries Research, 1984
Immunoglobulin A (IgA) protease, a family of bacterial enzymes, cleaves human IgA1 at a single bond generating distinct Fab and Fc fragments. Purified secretory IgA with known specificity for Streptococcus mutans NCTC 10449 (serotype c) was hydrolyzed with IgA protease prepared from Streptococcus sanguis ATCC 10556.
C P, Mallett, R J, Boylan, D L, Everhart
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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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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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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
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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
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