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- W2013431942 abstract "Glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate: NAD+ 2-oxidoreductase, EC 1.1.1.8) was isolated from rat brain tissue and its physical and kinetic properties investigated. The purification method resulted in the separation of fractions enriched for six other brain proteins and this procedure is presented. The apparent Michaelis constant (Km) for dihydroxyacetone phosphate is 0.17 mM whereas the Km for l-glycerol-3-phosphate is 0.30 mM. Under the conditions of the assay, the pH optimum occurs at pH 7.15. The molecular weight determined by Sephadex G-100 chromatography is 72 000 whereas ultracentrifugation in a sucrose gradient yields a molecular weight of 75 000. Furthermore using an antiserum prepared against purified rat brain glycerol-3-phosphate dehydrogenase, it was shown that rat brain glycerol-3-phosphate dehydrogenase is lighter than rabbit muscle glycerol-3-phosphate dehydrogenase (Mr 78 000). The purified enzyme is extremely sensitive to p-mercuribenzoate, being demonstrably inhibited by 10 nM, although it is much less sensitive to N-ethylmaleimide and iodoacetate. The specific activity of the purified enzyme is 152 units/mg of protein, representing a 2800-fold increase in specific activity. Analytical acrylamide gel electrophoresis separates the purified enzyme into two bands of protein, each of which exhibits glycerol-3-phosphate dehydrogenase activity. The isozymes differ from each in charge and neither one represents an oligomeric form of the other." @default.
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- W2013431942 date "1974-09-01" @default.
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- W2013431942 title "Purification and characterization of rat brain glycerol phosphatase dehydrogenase" @default.
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- W2013431942 doi "https://doi.org/10.1016/0005-2744(74)90128-4" @default.
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