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- W2092299355 abstract "1.1. Glucose 6-phosphate dehydrogenase was partially purified from Eimeria stiedai via differential salt precipitation and ion-exchange chromatography.2.2. Preservation of activity required NADP and a thiol-protector.3.3. The enzyme was specific for NADP.4.4. The forward rate was strongly influenced by various anions and divalent cations, increased with temperature to ca. 55°C and became erratic before declining at 60°C. Buffer composition strongly influenced the temperature effects.5.5. NADP at 1 mM conferred partial protection against thermal inactivation.6.6. The enzyme was unstable below pH 6.0, and the rate as a function of pH varied according to the buffer." @default.
- W2092299355 created "2016-06-24" @default.
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- W2092299355 date "1976-01-01" @default.
- W2092299355 modified "2023-10-16" @default.
- W2092299355 title "Partial purification and some properties of glucose 6-phosphate dehydrogenase from Eimeria stiedai (Lindemann, 1865) Kisskalt & Hartmann, 1907 (Protozoa: Coccidia)" @default.
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- W2092299355 doi "https://doi.org/10.1016/0305-0491(76)90136-x" @default.
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