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• W2329149817 abstract "A method is described for the purification of the enzyme phosphoenolpyruvate carboxykinase (PEPCK) from the cestode Hymenolepis diminuta. When purified to electrophoretic homogeneity, the enzyme had a molecular weight of 70,600 and an isoelectric point of 7.5. Kinetic studies indicated that the pH 5.6 was optimal for the carboxylation reaction and that Mn++ was the preferred divalent cation; there was no activity of the enzyme in the presence of Mg++. Apparent Km values for the carboxylation reaction were determined; those for GDP (20.6 muM) and PEP (38.9 muM) were lower than the values previously reported. GTP, GMP, ITP, IMP, fumarate, succinate and alpha-ketoglutarate were found to be competitive inhibitors and their Ki values determined." @default.
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• W2329149817 date "1981-12-01" @default.
• W2329149817 modified "2023-09-27" @default.
• W2329149817 title "Purification and Properties of Phosphoenolpyruvate Carboxykinase from Hymenolepis diminuta (Cestoda)" @default.
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• W2329149817 doi "https://doi.org/10.2307/3280707" @default.
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