Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1988639 | Journal of Biochemical and Biophysical Methods | 2006 | 11 Pages |
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.
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Authors
Zoltán Bicskei, Pilvi Ylander, Pekka Hänninen,