Related Experiment Video
Updated: Aug 11, 2026

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
Published on: August 15, 2013
Quantitative reappraisal of general expressions for multivalent protein binding in subunit-exchange chromatography
1Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville 32610.
Abstract:
Quantitative expressions have been derived for bivalent equilibria with immobilized ligand systems and for the equilibria for an immobilized protein whose self-association is modified by binding with a soluble ligand, as analyzed by affinity chromatography. These general expressions have been applied in a reexamination of multivalency in the affinity chromatography of antibodies, as reported by Eilat and Chaiken (Biochemistry 18 (1979) 790) and also to studies of neurophysin-peptide hormone interactions using glass matrices reported by Swaisgood and Chaiken (Biochemistry 25 (1986) 4148).
More Related Videos
10:41Ion Exchange Chromatography (IEX) Coupled to Multi-angle Light Scattering (MALS) for Protein Separation and Characterization
Published on: April 5, 2019
11:38Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022