Regulatory phosphorylation of the Na+/K(+)-ATPase from mammalian kidneys and Xenopus oocytes by protein kinases. Characterization of the phosphorylation site for PKC.
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Max-Planck-Institute for Biophysics, Frankfurt/M, Germany. 100304.1621@compuserve.com
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D000818:Animals; D001921:Brain / Q000201:enzymology; D005260:Female; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008322:Mammals; D016297:Mutagenesis, Site-Directed; D009865:Oocytes / Q000201:enzymology*; D010042:Ouabain / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012413:Rubidium / Q000378:metabolism; D012694:Serine; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014982:Xenopus laevis
D011994:Recombinant Proteins; D012694:Serine; D010042:Ouabain; D011493:Protein Kinase C; D000254:Sodium-Potassium-Exchanging ATPase; D012413:Rubidium; D013755:Tetradecanoylphorbol Acetate