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- W971561907 abstract "Publisher Summary This chapter discusses the methods for the enzymic microassays for D-mannose, D-glucose, D-galactose, L-fucose, and D-glucosamine in sugar mixtures. D-Mannose is phosphorylated to D-mannose 6-phosphate by hexokinase and ATP, and the production of ADP is measured using pyruvate kinase and lactic dehydrogenase. The extent of NADH oxidation is measured spectrophotometrically. The method is not specific for D-mannose since D-glucosamine, D-glucose, D-fructose, and 2-deoxy-D-glucose are also phosphorylated by hexokinase. This difficulty can be overcome by removing D-glucosamine with a cation exchange resin prior to assay and by measuring D-glucose with glucose-6-phosphate dehydrogenase; if glucose is present in the mixture, the appropriate correction is applied to the mannose assay. In the D-Glucose assay, the extent of NADP + reduction is measured spectrophotometrically. D-Galactose assay involves the reaction that can be catalyzed by D-galactose dehydrogenase. This assay is run at a relatively high pH, such that the galactonolactone is spontaneously hydrolyzed; the reaction thus becomes irreversible and proceeds to completion. The extent of NAD + reduction is measured spectrophotometrically. L-Fucose can be assayed with L-fucose dehydrogenase. At the high pH used for this assay, the fuconolaetone is spontaneously hydrolyzed and the reaction proceeds to completion. D-Glucosamine is removed from the sugar mixture by adsorption on a cation exchange resin. The glucosamine can then be eluted off the resin and assayed by the hexokinase-pyruvate kinase-lactic dehydrogenase assay described for D-mannose. The chapter describes the assays methods in brief." @default.
- W971561907 created "2016-06-24" @default.
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- W971561907 date "1975-01-01" @default.
- W971561907 modified "2023-10-14" @default.
- W971561907 title "[1] Enzymic microassays for d-mannose, d-glucose, d-galactose, l-fucose, and d-glucosamine" @default.
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- W971561907 doi "https://doi.org/10.1016/s0076-6879(75)41003-5" @default.
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