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Mammalian Phosphoprotein Phosphatase
Nature, 1962THE demonstration by Harris1 and Barth et al.2,3 of an enzyme in frog egg releasing phosphate from an endogenous phosphoprotein substrate was followed by the observation4 that mammalian tissue preparations split the phosphate bonds of exogenous phosphoproteins such as casein and phosvitin, at acid pH, at rates of about 60 µmoles phosphoprotein ...
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1986
Publisher Summary This chapter presents the classification and properties of cytoplasmic phosphoseryl-, phosphothreonyl-, as well as the phosphotyrosyl-protein phosphatases. A breakthrough in the area of phosphatase categorization occurred when Lee et al.
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Publisher Summary This chapter presents the classification and properties of cytoplasmic phosphoseryl-, phosphothreonyl-, as well as the phosphotyrosyl-protein phosphatases. A breakthrough in the area of phosphatase categorization occurred when Lee et al.
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Tyrosine Phosphoprotein Phosphatases
1998Abstract Tyrosine phosphoprotein phosphatases (PTPases) are found ubiquitously in cytosolic and particulate fractions of cells. They are unique in terms of their substrate sensitivity, neutral pH optimum, resistance to EDTA, and inhibition by low concentrations of zinc or vandanate.
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A phosphoprotein phosphatase in the chick embryo
Archives of Biochemistry and Biophysics, 1953M W, FOOTE, C A, KIND
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