Abstract
Nucleoli from Novikoff hepatoma ascites cells contain phosphatase activity that acts upon 32P-labeled nucleolar protein substrates. The activity is optimal near pH 7.0 and is inhibited by increasing concentrations of NaCl. The divalent cations CaCl 2, MnCl 2 and CoCl 2 at 6 mM inhibited phosphatase activity from 30–60%. ZnCl 2 completely inhibited the activity above 2 mM while EDTA and MgCl 2 had little effect. The activity was stimulated by dithiothreitol and inhibited by N-ethylmaleimide indicating a requirement for free sulfhydryl groups.
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