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- W290359305 abstract "We present a method of determining the affinity constant of a receptor-ligand pair using equilibrium binding in a microfluidic channel. This technique involves the immobilization of the receptor to the microchannel surface and perfusion of the ligand at a fixed flow rate. The ligand concentration in the eluent is monitored in real time. The break-through time of the ligand is then determined and compared with that of an appropriate, non-binding, reference molecule. The difference in break-through time can then be used in a mathematical model we have developed to determine the affinity constant of the receptor-ligand pair. Using this method, we have determined the equilibrium dissociation constant, K D , of a rat anti-insulin immunoglobulin and a fluorescein-conjugated human insulin. Fluorescein-conjugated aprotinin was used as the non-binding reference molecule. Our experiments yielded a K D value of 0.76 µM for this anti-insulin IgG and insulin-FITC pair." @default.
- W290359305 created "2016-06-24" @default.
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- W290359305 date "2009-03-13" @default.
- W290359305 modified "2023-09-27" @default.
- W290359305 title "Determination of Affinity Constant from Microfluidic Binding Assay" @default.
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- W290359305 doi "https://doi.org/10.1007/978-3-540-92841-6_221" @default.
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