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- W2030606942 abstract "Three major phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activities (I–III) from reticulocytes were resolved by DEAE-cellulose chromatography and fractionated further by chromatography on Sephacryl S-200. The major activity in each fraction had similar properties and was designated the B form Mr 270 000). This form constituted approximately 80% of the total phosphatase activity; approximately 15% of the activity was presented as the C form (Mr 140 000). Two other forms, D (Dr 180 000) and A (Mr > 500 000) were observed in minor amounts. All of the activities dephosphorylated histone phosphorylated by cyclic AMP-regulated kinases and casein phosphorylated by casein kinase II. When the B and C forms were examined further, a broad pH optimum between 7 and 8 was observed with histone; manganese stimulated dephosphorylation of histone with the B form but was required with the C form. Using casein as substrate, two pH optima, 5.6 and 7.5, were observed with the B form in the presence of manganese. In the absence of manganese, phosphatase activity with casein was observed only at pH 5.6. The C form was minimally active with casein. Phosphatase B was stimulated by treatment with trypsin and by freezing and thawing in the presence of mercaptoethanol; phosphatase C was either not affected or inhibited by these treatments. At high concentrations (4 mM) several small molecular weight compounds including ATP, GTP, glucose 6-phosphate and NaF were found to inhibit the B and the C forms. Cyclic AMP and hemin had little or no effect on the activities of phosphatase B and C with casein or histone as substrate." @default.
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- W2030606942 date "1980-02-01" @default.
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- W2030606942 title "Multiple forms of phosphoprotein phosphatase from rabbit reticulocytes" @default.
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- W2030606942 doi "https://doi.org/10.1016/0005-2744(80)90070-4" @default.
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