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Thermodynamic model of binding of flexible bivalent haptens to antibody

Abstract

Studies by Wilder et al. of the binding of Fab' fragments to small haptens have shown that the cross-linking constant (the equilibrium constant for binding an additional Fab' fragment to a hapten-Fab' complex) is strongly dependent on the length of the hapten. We present a simple model for predicting the relationship between the intermolecular cross-linking constant and the monovalent hapten-antibody binding constant. In particular we used the model to obtain the dependence of the cross-linking constant on the length of th hapten, the depth to which the hapten fills th Fab' binding site, and the size of the Fab' fragment. To test the model, we devised expressions which allowed us to analyze the data of Wilder et al. From their data we determined the values of two parameters which we took to be unknown in the theory, the size of the Fab' fragment and the depth to which the hapten fills the Fab' binding site. The values arrived at in this way agreed well with published measurements of these parameters.
Publication Date:
Jan 01, 1978
Product Type:
Journal Article
Reference Number:
ERA-04-055554; EDB-79-120185
Resource Relation:
Journal Name: Immunochemistry; (United Kingdom); Journal Volume: 15
Subject:
59 BASIC BIOLOGICAL SCIENCES; ANTIGEN-ANTIBODY REACTIONS; THERMODYNAMICS; BINDING ENERGY; COMPARATIVE EVALUATIONS; CROSS-LINKING; DATA; IMMUNOLOGY; SPATIAL DISTRIBUTION; CHEMICAL REACTIONS; DISTRIBUTION; ENERGY; INFORMATION; POLYMERIZATION; 550000* - Biomedical Sciences, Basic Studies
OSTI ID:
6138048
Research Organizations:
Los Alamos Scientific Lab., NM
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: IMCHA
Submitting Site:
TIC
Size:
Pages: 307-313
Announcement Date:

Citation Formats

Dembo, M, and Goldstein, B. Thermodynamic model of binding of flexible bivalent haptens to antibody. United Kingdom: N. p., 1978. Web. doi:10.1016/0161-5890(78)90091-3.
Dembo, M, & Goldstein, B. Thermodynamic model of binding of flexible bivalent haptens to antibody. United Kingdom. doi:10.1016/0161-5890(78)90091-3.
Dembo, M, and Goldstein, B. 1978. "Thermodynamic model of binding of flexible bivalent haptens to antibody." United Kingdom. doi:10.1016/0161-5890(78)90091-3. https://www.osti.gov/servlets/purl/10.1016/0161-5890(78)90091-3.
@misc{etde_6138048,
title = {Thermodynamic model of binding of flexible bivalent haptens to antibody}
author = {Dembo, M, and Goldstein, B}
abstractNote = {Studies by Wilder et al. of the binding of Fab' fragments to small haptens have shown that the cross-linking constant (the equilibrium constant for binding an additional Fab' fragment to a hapten-Fab' complex) is strongly dependent on the length of the hapten. We present a simple model for predicting the relationship between the intermolecular cross-linking constant and the monovalent hapten-antibody binding constant. In particular we used the model to obtain the dependence of the cross-linking constant on the length of th hapten, the depth to which the hapten fills th Fab' binding site, and the size of the Fab' fragment. To test the model, we devised expressions which allowed us to analyze the data of Wilder et al. From their data we determined the values of two parameters which we took to be unknown in the theory, the size of the Fab' fragment and the depth to which the hapten fills the Fab' binding site. The values arrived at in this way agreed well with published measurements of these parameters.}
doi = {10.1016/0161-5890(78)90091-3}
journal = {Immunochemistry; (United Kingdom)}
volume = {15}
journal type = {AC}
place = {United Kingdom}
year = {1978}
month = {Jan}
}