The Relation of Some Antigenic Determinants of Immunoglobulin G to the Non-L Chain Portion of the Fab Fragment

Vox Sanguinis ◽  
1968 ◽  
Vol 14 (1) ◽  
pp. 43-56
Author(s):  
R. Wolf ◽  
B. Wulf ◽  
H. Deicher
Keyword(s):  
Immunoglobulin G ◽  
Antigenic Determinants ◽  
Fab Fragment

scholarly journals A second rabbit kappa isotype.

1982 ◽  
Vol 156 (2) ◽  
pp. 585-595 ◽  
Author(s):  
A Benammar ◽  
P A Cazenave
Keyword(s):  
Light Chain ◽  
Immunoglobulin G ◽  
Antigenic Determinants ◽  
Gene Encoding ◽  
Genetic Studies ◽  
B Locus ◽  
Different Populations ◽  
Domestic Rabbits ◽  
Chain Type

Immunoglobulin G (IgG) from the rabbit strain Basilea was previously shown to contain two distinct populations of molecules one with light chain belonging to the known lambda isotype and the others to a new kappa-like L chain type. Alloantisera prepared against the Basilea IgG are directed against the kappa-like light chain (anti-bas antisera). All Basilea rabbits express kappa-like chains recognized by anti-bas sera, but IgG from other domestic rabbits did not react with these antisera. Genetic studies of wild rabbits belonging to different populations show that the bas+ phenotype could be found in heterozygous rabbits as well as those homozygous at the b locus. The gene encoding the bas+ light chain is closely linked to the b locus. Moreover, antigenic determinants recognized by anti-bas antibodies and antigenic determinants recognized by antibodies directed against allotypic determinants of the b series are located on distinct IgG molecules. These results show that there are two rabbit kappa isotypes: the kappa 1 isotype, bearing allotypic determinants of the b series, and the kappa 2 isotype, for which bas+ chain is one of the allotypic forms. The kappa 1 and kappa 2 isotypes are controlled by closely linked genes.

scholarly journals Studies on the antigenic determinants in the self-association of IgG rheumatoid factor

1981 ◽  
Vol 154 (1) ◽  
pp. 112-125 ◽  
Author(s):  
FA Nardella ◽  
DC Teller ◽  
M Mannik
Keyword(s):  
Sedimentation Equilibrium ◽  
Antigenic Determinants ◽  
Fab Fragment ◽  
Fab Fragments ◽  
Polymer Formation ◽  
Igg Rheumatoid Factor ◽  
Normal Human ◽  
Self Association ◽  
Equilibrium Ultracentrifugation ◽  
Antigen Antibody

The number, location, and other characteristics of the antigenic determinants for self-association of IgG-rheumatoid factors (IgG-RF) were examined using the IgG-RF isolated from the plasma of one patient as a model system. Affinity chromatography was employed for isolation of the IgG-RF. Sedimentation equilibrium ultracentrifugation was used to study the various interactions. The antigenic valence of IgG-RF Fc, normal human Fc, and rabbit Fc fragments was two for the interaction with Fab fragments from IgG-RF, as might be expected from the molecular symmetry of IgG. The antigenic valence of intact normal IgG, however, was only one, indicating that when one of the available antigenic determinants interacted with the Fab fragment of IgG-RF, the other determinant becomes sterically inaccessible. Reduction and alkylation, known to increase the flexibility of the hinge region, did not alter the antigenic valence of IgG for Fab fragments of IgG-RF. The antigenic valence of IgG-RF in self-association could not be experimentally determined but must be two to permit the observed concentration-dependent further polymer formation of IgG-RF dimers. Unique antigenic determinants on the Fc fragments of IgG-RF were sought and not found, thus reaffirming the formation of two antigen-antibody bonds as the basis for dimerization of IgG-RF molecules. The pFc' and Fc' fragments, representing Cγ3 domains of IgG, failed to show significant interaction with Fab fragments of IgG-RF, indicating that the antigenic determinants were not expressed by the Cγ3 regions but are located either on Cγ2 region or require intact Cγ2 and Cγ3 regions for expression. These conclusions were corroborated by the antigenic valence of one for the Fc(i) fragment, a new papain-generated intermediate fragment of Fc, composed of two intact Cγ3 domains and one intact Cγ2 domain. Normal IgG, because of its valence of one for interaction with IgG-RF, would effectively terminate further polymerization of IgG-RF dimers. This may well in part explain the finding of smaller IgG-RF complexes in the serum than in synovial fluid of patients with rheumatoid arthritis.

A radioimmunoassay specific for the antigenic determinants exposed by pepsin digestion of human immunoglobulin G

1974 ◽  
Vol 11 (9) ◽  
pp. 573-579 ◽  
Author(s):  
Robert J. Carrico ◽  
Robert Beagle ◽  
Magdalena Usategui-Gomez ◽  
Friedrich Deinhardt
Keyword(s):  
Immunoglobulin G ◽  
Human Immunoglobulin ◽  
Antigenic Determinants ◽  
Pepsin Digestion ◽  
Human Immunoglobulin G

scholarly journals Structure of a factor VIII C2 domain–immunoglobulin G4κ Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII

Blood ◽  
2001 ◽  
Vol 98 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Paul Clint Spiegel ◽  
Marc Jacquemin ◽  
Jean-Marie R. Saint-Remy ◽  
Barry L. Stoddard ◽  
Kathleen P. Pratt
Keyword(s):  
Factor Viii ◽  
B Lymphocyte ◽  
Antigenic Determinants ◽  
C2 Domain ◽  
Inhibitory Antibody ◽  
Fab Fragment ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Lymphocyte Cell ◽  
Lymphocyte Cell Line

Abstract The development of an immune response to infused factor VIII is a complication affecting many patients with hemophilia A. Inhibitor antibodies bind to antigenic determinants on the factor VIII molecule and block its procoagulant activity. A patient-derived inhibitory immunoglobulin G4κ antibody (BO2C11) produced by an immortalized memory B-lymphocyte cell line interferes with the binding of factor VIII to phospholipid surfaces and to von Willebrand factor. The structure of a Fab fragment derived from this antibody complexed with the factor VIII C2 domain was determined at 2.0 Å resolution. The Fab interacts with solvent-exposed basic and hydrophobic side chains that form a membrane-association surface of factor VIII. This atomic resolution structure suggests a variety of amino acid substitutions in the C2 domain of factor VIII that might prevent the binding of anti-C2 inhibitor antibodies without significantly compromising the procoagulant functions of factor VIII.

scholarly journals ANTIGENIC DETERMINANTS RESULTING FROM POLYMERIZATION OF IMMUNOGLOBULIN G

1988 ◽  
Vol 41 (5-6) ◽  
pp. 189-196 ◽  
Author(s):  
Kayoko ARAI ◽  
Junichi YASUDA ◽  
Takako SASAKI ◽  
Kunio YONEMASU
Keyword(s):  
Immunoglobulin G ◽  
Antigenic Determinants

scholarly journals Ultrastructural localization of gamma-chain and immunoglobulin G in human lymphocytes using enzyme-labeled Fab fragment.

1975 ◽  
Vol 23 (8) ◽  
pp. 624-631 ◽  
Author(s):  
C T Lin ◽  
J P Chang ◽  
J P Chen
Keyword(s):  
Endoplasmic Reticulum ◽  
Immunoglobulin G ◽  
Human Lymphocytes ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Gamma Chain ◽  
Fab Fragment ◽  
Peripheral Lymphocytes ◽  
Human Peripheral Lymphocytes ◽  
Normal Human

By the use of rabbit antibodies against the heavy chain of human immunoglobulin G (IgG), the gamma-chain and IgG molecules were successfully localized at the ultrastructural level in human peripheral lymphocytes. The rabbit Fab fragment was coupled to horseradish peroxidase by means of glutaraldehyde and the resulting conjugate could penetrate the intact plasma membrane. Discernible reaction product was observed in cisternae of the nuclear envelope, rough endoplasmic reticulum and Golgi apparatus as well as on the surface of the lymphocytes. In normal human individuals under no specific antigenic stimulation, only a few peripheral lymphocytes showed a rare positive intractoplasmic reaction. Reaction product may represent either the whole IgG molecule, the half molecule consisting of one heavy and one light chain or nascent gamma-chain.

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