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- W265578265 abstract "Publisher Summary This chapter discusses the procedure for measuring nanomole to picomole amounts of NADH, NADPH, and FMN. Purified bacterial luciferase is used for the procedure, and this is available commercially. Most preparations contain the dehydrogenase, which promotes light production some 20 times more efficiently with NADH than with NADPH. Thus, the sensitivity of the assay of NADPH is only 5% of that for NADH. A liquid-scintillation spectrometer is a suitable unit for measuring the number of photons produced, as are a number of sensitive photometers marketed to measure chemiluminescence and bioluminescence. Quantitation is effected by ensuring that the component to be measured is the only rate-limiting item of the coupled-enzyme reaction. Because currently commercially available luciferase preparations are only partially purified, the interference in assays by contaminating enzymes should be assessed using appropriate controls." @default.
- W265578265 created "2016-06-24" @default.
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- W265578265 date "1978-01-01" @default.
- W265578265 modified "2023-10-16" @default.
- W265578265 title "[24] Quantitation of picomole amounts of NADH, NADPH, and FMN using bacterial luciferase" @default.
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- W265578265 doi "https://doi.org/10.1016/0076-6879(78)57026-2" @default.
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