Inhibition by lead ion of Electrophorus electroplax (Na+ + K+)-adenosine triphosphatase and K+-p-nitrophenylphosphatase.
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Inhibition by lead ion of Electrophorus electroplax (Na+ + K+)-adenosine triphosphatase and K+-p-nitrophenylphosphatase.
Inorganic lead ion in micromolar concentrations inhibits Electrophorus electroplax microsomal (Na+ + K+)-adenosine triphosphatase ((Na+ + K+)-ATPase) and K+-p-nitrophenylphosphatase (NPPase). Under the same conditions, the same concentrations of PbCl2 that inhibit ATPase activity also stimulate the phosphorylation of electroplax microsomes in the absence of added Na+. Enzyme activity is protect...
متن کاملInhibition by Lead Ion of EZectrophorus Electroplax (Na+ + K+)-Adenosine Triphosphatase and K+-p- Nitrophenylphosphatase*
Inorganic lead ion in micromolar concentrations inhibits Electrophorus electroplax microsomal (Na+ + K+)-adenosine triphosphatase ((Na+ + K+)-ATPase) and K+-p-nitrophenylphosphatase (NPPase). Under the same conditions, the same concentrations of PbCl, that inhibit ATPase activity also stimulate the phosphorylation of electroplax microsomes in the absence of added Na+. Enzyme activity is protect...
متن کاملIrreversible zinc ion inhibition of (Na+ -K+)-adenosinetriphosphatase, Na+ -phosphorylation, and K+-p-nitrophenylphosphatase of Electrophorus electricus electroplax.
Zinc ion in micromolar concentrations is an irreversible inhibitor of Elrcrrophorus ulccrricws electroplax microsomal (Na+-K *)-ATPase. The rate of inhibition is dependent on [ZnCIJ and the extent of inhibition varies with thc ratio of ZnClz to microsomal protein. The same kinetics are obsmcd for inhibition of K +-p-nitrophenylphosphatase and steady-state levels of Na'-dependent enzyme phosphor...
متن کاملLead ion activates phosphorylation of electroplax Na+- and K+-dependent adenosine triphosphatase ((NaK)-ATPase) in the absence of sodium ion.
PbCl, in micromolar concentrations stimulates phosphorylation of electroplax microsomal protein in the absence of Nat. Other divalent cations showed little or no such effect. The (Mg’+ + Pb’+)and (Mg”+ + Na+)-dependent membrane-bound protein kinase activities in electroplax particulate preparations exhibit properties in common, including their acid stability, ouabain sensitivity, ATP specificit...
متن کاملReaction of (Na+ + K+)-dependent adenosine triphosphatase with inorganic phosphate. Regulation by Na+, K+, and nucleotides.
Effects of Na+, K+, and nucleotides on Mg2+-dependent phosphorylation of (Na+ + K+)-dependent adenosine triphosphatase by Pi were studied under equilibrium conditions. Na+ was a linear competitive inhibitor with respect to Mg2+ and a mixed inhibitor with respect to Pi. K+ was a partial inhibitor; it interacted with positive cooperativity and induced negative cooperativities in the interactions ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63331-4