Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System
AbstractWe used the interaction between human serum albumin (HSA) and a high-affinity antibody to evaluate binding affinity measurements by the bench-top liSPR system (capitalis technology GmbH). HSA was immobilized directly onto a carboxylated sensor layer, and the mechanism of interaction between the antibody and HSA was investigated. The bivalence and heterogeneity of the antibody caused a complex binding mechanism. Three different interaction models (1:1 binding, heterogeneous analyte, bivalent analyte) were compared, and the bivalent analyte model best fit the curves obtained from the assay. This model describes the interaction of a bivalent analyte with one or two ligands (A + L ↔ LA + L ↔ LLA). The apparent binding affinity for this model measured 37 pM for the first reaction step, and 20 pM for the second step. View Full-Text
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Henseleit, A.; Pohl, C.; Kaltenbach, H.-M.; Hettwer, K.; Simon, K.; Uhlig, S.; Haustein, N.; Bley, T.; Boschke, E. Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System. Biosensors 2015, 5, 27-36.
Henseleit A, Pohl C, Kaltenbach H-M, Hettwer K, Simon K, Uhlig S, Haustein N, Bley T, Boschke E. Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System. Biosensors. 2015; 5(1):27-36.Chicago/Turabian Style
Henseleit, Anja; Pohl, Carolin; Kaltenbach, Hans-Michael; Hettwer, Karina; Simon, Kirsten; Uhlig, Steffen; Haustein, Natalie; Bley, Thomas; Boschke, Elke. 2015. "Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System." Biosensors 5, no. 1: 27-36.