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Updated: May 23, 2025

Autoradiography as a Simple and Powerful Method for Visualization and Characterization of Pharmacological Targets
Published on: March 12, 2019
A straightforward method for measuring binding affinities of ligands to proteins of unknown concentration in
Bin Yan1, Josephine Bunch1,2
1National Centre of Excellence in Mass Spectrometry Imaging, National Physical Laboratory Hampton Road Teddington TW11 0LW UK bin.yan@npl.co.uk.
Abstract:
The equilibrium dissociation constant (K d) is a quantitative measure of the strength with which a drug binds to its receptor. Methods for determining K d typically require a priori knowledge of protein concentration or mass. We report a simple dilution method for estimation of K d using native mass spectrometry which can be applied to protein-ligand complexes involving proteins of unknown concentration, from complex mixtures, including direct tissue sampling.
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