Calibration of bioaffinity assays using kinetic data

Journal of Biochemical and Biophysical Methods
Zoltán BicskeiPekka Hänninen

Abstract

Bioaffinity assays are usually calibrated by using a set of standard measurements fitted to a simple empirical model. In this paper, a new calibration approach based on mechanistic model of reaction kinetics is presented. When the calibration assay is known in terms of reaction mechanism, incubation time, initial concentration, and rate constants, one can back-calculate concentrations of unknown samples measured in a nonequilibrium time point. This paper describes a calculation method of unknown sample concentrations based on kinetically measured single calibration assay point. The theoretical results are verified by two common in-vitro diagnostic assays.

References

Feb 1, 1997·Journal of Immunoassay·E ZuberJ P Flandrois
Aug 15, 1997·Analytical Biochemistry·E ZuberJ P Flandrois
May 10, 2000·Nature Biotechnology·P HänninenE Soini
Apr 15, 2004·Analytical Biochemistry·Andrew W DrakeScott L Klakamp

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Citations

Oct 11, 2008·Clinical Chemistry and Laboratory Medicine : CCLM·Luis Antonio Tortajada-Genaro, Monica Romero
Jul 4, 2008·Annals of the New York Academy of Sciences·Pekka HänninenJuhani T Soini
Mar 30, 2018·Annual Review of Analytical Chemistry·David GasperinoBernhard H Weigl
Oct 23, 2019·The Journal of Applied Laboratory Medicine·Mark A ZaydmanAnn M Gronowski

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