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- W416915809 abstract "This chapter describes optical biosensors based on enzyme–substrate complex formation. The classical biosensor uses a specific oxidase to catalyze the transfer of electrons from the analyte to an electrode surface, yielding a current proportional to the reaction rate and thence to the analyte concentration. It is found that although considerable research effort has gone into the refinement of this basic design, no general solution has been found to the problem of nonspecific oxidation of interfering substances at the electrode surface. One way of circumventing this problem is to exploit the substrate-binding properties of the enzyme rather than the complete enzyme-catalyzed reaction. The application of this principle to the development of biosensors for theophylline, and for salicylate, both of which are analytes of clinical significance is reported. Theophylline oxidase is a hem-containing enzyme which catalyzes the oxidation of theophylline by cytochrome C. In the absence of cytochrome C, the formation of the enzyme–theophylline complex can be monitored by the resulting reduction of the enzymes own hem group." @default.
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- W416915809 date "1994-01-01" @default.
- W416915809 modified "2023-09-23" @default.
- W416915809 title "Optical Biosensors Based on Enzyme-Substrate Complex Formation" @default.
- W416915809 doi "https://doi.org/10.1016/b978-1-85617-242-4.50103-8" @default.
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