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Updated: Aug 15, 2026

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Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Published on: February 15, 2018
Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with
Katrina High1, Yuan Meng, Michael W Washabaugh
1Department of Bioprocess and Bioanalytical Research, Merck Research Laboratories, West Point, PA 19486, USA.
Analytical Biochemistry
|October 19, 2005
Abstract
No abstract available in PubMed .
Related Concept Videos
Enzyme-Linked Immunosorbent Assay
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
The Equilibrium Binding Constant and Binding Strength
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

