The Affinity of Antibody: Range, Variability, and the Role of Multivalence

Karush, Fred

doi:10.1007/978-1-4684-0805-8_3

Cited by 86 publications

(62 citation statements)

References 79 publications

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“…Association rate constants were in the range 105-106m-1 s-1, and thus of similar magnitude to k+ values for antibody-protein antigen interactions (Karush, 1978) or for the interaction immunoglobulin E with its receptor on mast cells (Kulczycki & Metzger, 1974). All these values are about two orders of magnitude smaller than those determined for antibody-hapten reactions (Day et al, 1963;Karush, 1978). Part of this difference may be due to differences in diffusion coefficients, which are approximately proportional to (molecular weight)-l. However, it is clear that other factors must also be important in determining association rate constants of antibody-antigen interactions.…”

Section: Discussionmentioning

confidence: 60%

“…Part of this difference may be due to differences in diffusion coefficients, which are approximately proportional to (molecular weight)-l. However, it is clear that other factors must also be important in determining association rate constants of antibody-antigen interactions. Even for the same hapten there can be a wide range of k+1 values (Karush, 1978), and differences in diffusion rate cannot explain the 14-fold difference between k+1 values for W3/13 and W3/25 antibodies interacting with cell surfaces. The practical consequences of low and variable k+1 values for the interpretation of absorption analyses are illustrated by the results obtained with W3/13 and W3/25 antibodies (see section 10).…”

Section: Discussionmentioning

confidence: 99%

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The kinetics of antibody binding to membrane antigens in solution and at the cell surface

Mason¹,

Williams²

1980

Biochemical Journal

522

194

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The reaction kinetics of 251I-labelled mouse monoclonal antibodies binding to three cell-surface antigens of rat thymocytes (Thy-1.1, W3/13 and W3/25) were studied. The differences between bivalent and univalent interactions were determined by using antibody in the F(ab')2 or Fab' form and by using antigen in polymeric or monomeric forms. Association rate constants (k+ ), dissociation rate constants (k-) and equilibrium constants were determined. Also, the dissociation kinetics of rabbit antibodies against rat Thy-i antigen were studied. The major findings were as follows. (i) With F(ab')2 antibody there was no simple relationship between antigen density at the cell surface and extent of bivalent binding. Extensive univalent binding was observed unless the antibody had a high k-, for the univalent interaction, in which case all binding was bivalent.(ii) k+1 values were similar for F(ab')2 or Fab' antibody, and for the different antibodies were in the range 0.8 x 105-1.1 x 106M-1s-1. These differences were sufficient to affect the interpretation of serological assays with the different antibodies. (iii) Antibody bound bivalently dissociated much more slowly than that bound univalently.However, the k-, values for the univalently bound antibody were sufficiently low in most cases that the lifetime of the univalent complex was similar to or greater than the time needed for the assay. Thus the results could be interpreted on the basis of irreversible reactions. The overall conclusion from the study is that for an understanding of the binding of antibody to cell-surface antigens the kinetics of the interaction are of major importance and theories based on equilibrium binding are inappropriate.

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Section: Discussionmentioning

confidence: 60%

Section: Discussionmentioning

confidence: 99%

The kinetics of antibody binding to membrane antigens in solution and at the cell surface

Mason¹,

Williams²

1980

Biochemical Journal

522

194

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“…Since IgG antibodies produced for protein in an early stage of infection and for carbohydrates are known to possess a low affinity, such antibodies carry a high specificity that causes cross-reaction with a very similar or identical antigenic structure (7,16). Gilmore et al (10,11) demonstrated the cross-reactivity of rOmp B between SFG and TG and confirmed the ompB gene homology by Southern blot analysis using the cloned DNA of R. rickettsii ompB.…”

Section: Discussionmentioning

confidence: 99%

Cross‐Reactivity of Rickettsia japonica and Rickettsia typhi Demonstrated by Immunofluorescence and Western Immunoblotting

Uchiyama

Zhao

Yan-sheng

et al. 1995

Microbiology and Immunology

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Cross-reactivity between Rickettsia japonica and R. typhi was observed by immunofluorescence tests using sera from patients with Oriental spotted fever (OSF), from whom the causative agent was isolated and identified as R. japonica. Western immunoblotting with these sera revealed that only the 120-kilodalton surface polypeptide, i.e., rickettsial outer membrane protein (rOmp) B, has a common antigenicity with the 105-kilodalton surface polypeptide of R. typhi. In some cases, antibodies specifically reactive with R. typhi were detected in acute-phase sera followed by a significant rise in titers, possibly because of an anamnestic response to a previous infection with an R. typhi-like agent; the sera retained reactivity to R. typhi even after absorption by a homologous strain. A lipopolysaccharide (LPS)-like antigen of R. typhi was found to be reactive with some sera of OSF patients. The ladder bands on Western immunoblot of rickettsial organisms were confirmed to be polysaccharide in nature, which was demonstrated by comparing them with the pattern of silver-stained gel of proteinase K-treated rickettsial specimens after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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“…The immunological term avidity was coined more than fifty years ago to distinguish between the binding properties of an antibody and its monovalent Fab fragment (reviewed in (Karush, 1989)). It was observed that an IgG, at low concentrations, could bind to a surface containing multiple binding sites (epitopes) with an apparent affinity that was orders of magnitude greater than the equilibrium constant for binding of one of its Fab sites to an epitope (Gopalakrishnan & Karush, 1974;Greenbury et al, 1965;Hornick & Karusch, 1972).…”

Section: Introductionmentioning

confidence: 99%

Mathematical Modeling of Syk Activation in Allergen-Stimulated Mast Cells and Basophils

Nag¹,

Monine²,

Goldstein³

et al. 2012

Advances in Protein Kinases

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The Affinity of Antibody: Range, Variability, and the Role of Multivalence

Cited by 86 publications

References 79 publications

The kinetics of antibody binding to membrane antigens in solution and at the cell surface

The kinetics of antibody binding to membrane antigens in solution and at the cell surface

Cross‐Reactivity of Rickettsia japonica and Rickettsia typhi Demonstrated by Immunofluorescence and Western Immunoblotting

Mathematical Modeling of Syk Activation in Allergen-Stimulated Mast Cells and Basophils

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