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  • Title: A protein kinase of the plasma membrane of Dictyostelium discoideum.
    Author: Juliani MH, Klein C.
    Journal: Biochim Biophys Acta; 1981 Dec 15; 662(2):256-64. PubMed ID: 7317441.
    Abstract:
    D. discoideum amoebae were found to phosphorylate plasma membrane proteins when intact cells were incubated with either [gamma-32P]ATP or [32P]phosphate. In the first case, the incorporation was largely a consequence of the hydrolysis of [gamma-32P]ATP, cellular uptake of the generated [32P]phosphate and its subsequent incorporation into ATP. When the contribution of this process to the phosphorylating activity of intact cells was eliminated, an ecto-protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) activity could be demonstrated. As amoebae progressed through their aggregation program, they showed a decreased ability to phosphorylate their plasma membrane when incubated with [gamma-32 P]ATP or [32P]phosphate. Analysis of ATPase activity, permeability properties and the pattern of proteins phosphorylated by intact cells and isolated plasma membranes lead to the following conclusions: the lower levels of phosphorylation observed with starved cells reflected an altered uptake of [32P]phosphate by these cells rather than a significant change in the plasma membrane protein kinase activity. Neither the substrates nor the activity of the ecto-protein kinase was dramatically altered during starvation.
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