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Equilibrium dialysis question?

Equilibrium dialysis question?


1 Answers

askIITians Faculty 747 Points
6 years ago
Equilibrium dialysis is a specific application of dialysis that is important for the study of the binding of small molecules and ions by proteins. It is one of several methods available for this purpose, and its attractive feature continues to be its physical simplicity. Another attractive feature of equilibrium dialysis is the ability to perform interaction studies without the use of fluorescent or radiolabeled tags. Generally, the objective of an equilibrium dialysis experiment is to measure the amount of a ligand bound to a macromolecule. This is typically done through an indirect process because in any mixture of the ligand and macromolecule, it is difficult to distinguish between the bound and free ligand. If, however, the free ligand can be dialyzed through a membrane, until its concentration across the membrane is at equilibrium, the free ligand concentration can be measured easily. Data obtained under different experimental conditions then provides information on various binding parameters of the compounds such as the binding constants and the number of binding sites or binding capacity

Harvard Apparatus/AmiKa offers four types of Equilibrium DIALYZERS™. These products can meet virtually all of your bindinteraction application requirements: Micro-Equilibrium DIALYZER™ The Micro-Equilibrium DIALYZER is available as 2- or 3-chamber systems. It is used to study interactions between biomolecules such as the binding of a ligand to a protein. For sample volumes from 25µl to 500µl,
Multi-Equilibrium DIALYZER™ For simultaneous and highly reproducible equilibrium dialysis of up to 20 samples with volumes from 0.25 to 5ml,
DispoEquilibrium DIALYZER™ A disposable version of the Micro-Equilibrium DIALYZER suitable for samples from 25 to 75µl,
96-Well Equilibrium DIALYZER™ A 96-well disposable equilibrium DIALYZER for high throughput interaction studies. For samples up to 50µl to 200µl,

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