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Updated: Aug 15, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
The influence of product instability on slow-binding inhibition
C Garrido-Del Solo1, J M Yago, M García-Moreno
1Departamento de Química-Física, Escuela Politécnica Superior, Universidad de Castilla-La Mancha Avda, España, s/n Campus Universitario, E-02071 Albacete, Spain.
Abstract:
We present a kinetic study of an enzyme reaction that takes place with slow-binding inhibition where the immediate product undergoes a spontaneous or induced process of decomposition. A kinetic study of an enzyme process, in which a slow-binding inhibition process and a decomposition of the immediate product of the reaction take place simultaneously is performed. The corresponding explicit concentration-time equations were obtained. Using the analytical solutions obtained, which were tested numerically, we suggest a procedure that allows the discrimination between the particular cases considered and the evaluation of the principal kinetic parameters of the reaction.
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