Calibration of bioaffinity assays using kinetic data.
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.
Bicskei
Zoltán
Z
University of Turku, Institute of Biomedicine, Laboratory of Biophysics, Tykistökatu 6, FIN-20520 Turku, Finland.
Ylander
Pilvi
P
Hänninen
Pekka
P
D001681:Biological Assay / Q000592:standards*; D002097:C-Reactive Protein / Q000032:analysis; D002138:Calibration; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D013972:Thyrotropin / Q000032:analysis
D013972:Thyrotropin; D002097:C-Reactive Protein