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- W977105890 abstract "This chapter describes the assay method, purification procedure, and properties of L-arabino-aldose dehydrogenase. This dehydrogenase also catalyzes the oxidation of other aldoses possessing the L-arabino configuration at carbon atoms 2 through 4 (or their deoxy derivatives), and is believed to function in the metabolism of D-fucose, D-galactose, and L-arabinose in pseudomonad MSU-1. It is important to use NADP+ rather than NAD+ when assays are made on extracts of D-fucose-grown cells in order to prevent interference by o-aldohexose dehydrogenase. The enzyme is purified from pseudomonad MSU-1. The purification procedure steps are: protamine sulfate treatment, heat step, ammonium sulfate fractionation, sephadex G-200 chromatography, and calcium phosphate gel step. Except for the heat step, the following procedures are performed at 0° to 4°. Of 55 compounds tested as possible substrates, the only six that are oxidized by this enzyme are those that possess the L-arabino configuration and their deoxy derivatives. Both NAD and NADP serve as coenzymes. Km values at pH 8.1 are 15 μM for NAD+ and 68 μM for NADP+. Other properties are also discussed." @default.
- W977105890 created "2016-06-24" @default.
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- W977105890 date "1975-01-01" @default.
- W977105890 modified "2023-10-18" @default.
- W977105890 title "[35] l-arabino-aldose dehydrogenase" @default.
- W977105890 cites W1493701512 @default.
- W977105890 cites W1506043065 @default.
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- W977105890 doi "https://doi.org/10.1016/s0076-6879(75)41037-0" @default.
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