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- W1981004051 abstract "Abstract The native cell wall acid phosphatase fraction was eluted at 0.6 M sodium chloride from a column of isolated cell walls of tobacco XD-6S cells with a linear increasing gradient of sodium chloride. A 48-fold purification was obtained by protein fractionation with hydroxyapatite, DEAE-Sephacel and butyl-Toyopearl 650. Native electrophoresis showed a diffuse protein band corresponding to the enzyme activity. The K m of the enzyme for p -nitrophenyl phosphate ( p NPP) at pH 5.6 was 0.38 mM. The activation energy for the denaturation of hydrolysis activity was 10.4 kJ mol −1 in the range of 30–80°. The enzyme showed rather broad substrate specificity toward several compounds." @default.
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- W1981004051 date "1990-01-01" @default.
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- W1981004051 title "Purification and properties of native cell wall acid phosphatase from cultured tobacco cells" @default.
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- W1981004051 doi "https://doi.org/10.1016/0031-9422(90)87097-e" @default.
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