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  • Title: Measurement of biochemical affinities with a Gill titration calorimeter.
    Author: Harrous ME, Parody-Morreale A.
    Journal: Anal Biochem; 1997 Dec 01; 254(1):96-108. PubMed ID: 9398351.
    Abstract:
    A Gill titration calorimeter is evaluated as an instrument to determine in one experiment the equilibrium constant and the enthalpy change of a biochemical reaction. The dimensionless parameter kc (the product of the association equilibrium constant and the concentration of the reagent to be titrated; Wiseman et al., Anal. Biochem. 179, 131-137, 1989) is used to analyze the instrument performance. The analysis of simulated titration data corresponding to a simple model case shows that association equilibrium constants in the 10(2)-10(7) M-1 range may be determined when the kc parameter is between 1 and 1000. In addition we use a Monte Carlo approach to estimate the precision in the thermodynamic parameters of the reaction under study. The relative precision in the calculated constants ranges from 3 to 80% depending on the macromolecule concentration and kc value in the experiment. These results were checked with the study of the reactions of beta-trypsin with its inhibitor and ribonuclease A with cytidine 2'-monophosphate and cytidine 3'-monophosphate.
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