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- W2006483044 abstract "1. Phosphatase activities exerted on phosphoprotein (casein), inorganic pyrophosphate, β-glycerophosphate, p-nitrophenylphosphate and on various phosphomonoesters were demonstrated in homogenates of newborn-rat calvaria. The activity exerted on phosphoprotein was optimal below pH 5.8; with all the other substrates, two peaks of activity were observed, one between pH 4.8 and 5.8 and the other between pH 9 and 11. 2. The main kinetic characters of these phosphatases have been studied and methods for their quantitative assays have been developed. 3. Kinetic properties, stability characteristics and competitive inhibition experiments are interpreted as an indication of at least three different acid phosphatases in bone cells: phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16), acid β-glycerophosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.2) and acid inorganic pyrophosphatase, the latter enzyme being apparently responsible for the acid p-nitrophenylphosphatase activity of the homogenates." @default.
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- W2006483044 date "1973-01-01" @default.
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- W2006483044 title "The acid and alkaline phosphatases, inorganic pyrophosphatases and phosphoprotein phosphatase of bone. I. Characterization and assay" @default.
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- W2006483044 doi "https://doi.org/10.1016/0005-2744(73)90387-2" @default.
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