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- W1617990712 abstract "This chapter discusses the dihydroorotate dehydrogenase (Escherichia coli). The enzyme is membrane-bound and linked with the electron transport system of the cell. When the system is intact, the enzyme can therefore be assayed either as an oxidase or as a dehydrogenase. When the system is not intact, the enzyme can be assayed as a dehydrogenase using such electron acceptors as ferricyanide, various quinones, or 2,6-dichlorophenolindophenol (DCIP). The oxidase and DCIP-reducing methods are described in the chapter. Enzyme activity is determined spectrophotometrically by following the rate of absorbance increase at 290 nm, which is associated with the appearance of orotate. The enzyme is associated with the inner side of the bacterial cytoplasmic membrane. It can be detached from it by the action of phospholipase A2 (Naja naja or pig pancreatic enzyme) followed by the adjustment of the pH to 8.4. Enzyme solubilized in this way has, however, a strong tendency to form inactive aggregates." @default.
- W1617990712 created "2016-06-24" @default.
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- W1617990712 date "1978-01-01" @default.
- W1617990712 modified "2023-10-10" @default.
- W1617990712 title "[8] Dihydroorotate dehdydrogenase (Escherichia coli)" @default.
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- W1617990712 doi "https://doi.org/10.1016/s0076-6879(78)51010-0" @default.
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