Lead ion activates phosphorylation of electroplax Na+- and K+-dependent adenosine triphosphatase ((NaK)-ATPase) in the absence of sodium ion. |
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Authors: | G J Siegel S K Fogt |
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Institution: | Neurology Research Laboratory Neurology Department University of Michigan Ann Arbor, Michigan 48104 U.S.A. |
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Abstract: | PbCl2 in micromolar concentrations stimulates phosphorylation of electroplax microsomal protein in the absence of Na+. Other divalent cations showed little or no such effect. The (Mg2+ + Pb2+)- and (Mg2+ + Na+)-dependent membrane-bound protein kinase activities in electroplax particulate preparations exhibit properties in common, including their acid stability, ouabain sensitivity, ATP specificity, and molecular size. It is concluded that the (Mg2+ + Pb2+)-dependent phosphoprotein is part of the Na+-, K+-dependent adenosine triphosphatase (NaK)ATPase]. The Pb2+-dependent product, in contrast to the Na+-dependent one, is insensitive to K+ and the hydrolysis of ATP is thus inhibited. |
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