Results 181 to 190 of about 49,117 (237)
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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
openaire   +3 more sources

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.
M, de Boer   +3 more
openaire   +3 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   +4 more
openaire   +4 more sources

pH-responsive multi-network composite cellulose-based hydrogels for stable delivery of oral IgY-Fab fragments.

Food Chemistry, 2023
Yolk immunoglobulin (IgY) is perfect supplement to mammalian immunoglobulin G in passive immune protection but with poor delivery stability. This work succeeded in pH-responsive oral delivery of IgY-Fab fragments with cellulose based multi-network ...
Minquan Xia   +5 more
semanticscholar   +1 more source

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
openaire   +2 more sources

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   +3 more
openaire   +2 more sources

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   +3 more
openaire   +3 more sources

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
openaire   +2 more sources

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 ...
openaire   +2 more sources

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