Diversity of Regulatory Phosphorylation of the Na+/K+-ATPase from Mammalian Kidneys and Xenopus Oocytes by Protein Kinases: Characterization of the Phosphorylation Site for Protein Kinase C

Cellular Physiology and Biochemistry

Volumn 7, Issue 1, 1997, Pages 1-18

  Vasilets, Larisa A ^a,b  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b INSTITUTE OF PROBLEMS OF CHEMICAL PHYSICS   (Russian Federation)

Author keywords

Na+ K+ ATPase; Phosphorylation sites; Protein kinases; Site directed mutagenesis; Xenopus oocytes

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); MUTANT PROTEIN; PROTEIN KINASE C;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; DOG; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PHOSPHORYLATION; ENZYME REGULATION; KIDNEY; MAMMAL; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; SHEEP; SWINE; XENOPUS;

ANIMALIA; CANIS FAMILIARIS; MAMMALIA; OVIS ARIES; STROPHANTHUS GRATUS; SUS SCROFA;

EID: 0030857165     PISSN: 10158987     EISSN: 14219778     Source Type: Journal    
DOI: 10.1159/000154847     Document Type: Article

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