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- W1983315468 abstract "Three distinct inorganic pyrophosphatases with different pH optima have been isolated from thoracic muscle mitochondria of the American cockroach. Purification was achieved by sonication, differential centrifugation, ammonium sulphate fractionation, and column chromatography on Sephadex, DEAE† cellulose, and CM cellulose. Each of the enzymes required magnesium for maximal activation but the optimum magnesium to substrate ratio varied. The Michaelis constants were 1·2×10−3, 2×10−3, and 1·6×10−3 M for the acid, neutral, and alkaline pyrophosphatase, respectively. All three of the enzymes split inorganic phosphate from polyphosphate and GTP to some degree. In addition, the enzymes were inhibited by NaF, DNP, NaCN, and to a lesser extent by certain purine and pyrimidine nucleotides. Divalent metal ions also inhibited the reactions presumably by competing with available magnesium ions." @default.
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- W1983315468 date "1965-11-01" @default.
- W1983315468 modified "2023-09-23" @default.
- W1983315468 title "Isolation and properties of inorganic pyrophosphatases from cockroach thoracic muscle mitochondria" @default.
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- W1983315468 doi "https://doi.org/10.1016/0022-1910(65)90163-0" @default.
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