Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity

Journal of Biological Chemistry

Volumn 280, Issue 19, 2005, Pages 18736-18744

  Imagawa, Toshiaki ^a   Yamamoto, Tetsuya ^a   Kaya, Shunji ^a   Sakaguchi, Kazuyasu ^a   Taniguchi, Kazuya ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; ENZYME INHIBITION; ENZYMES; LIVING SYSTEMS STUDIES; SUBSTITUTION REACTIONS;

CELL LINES; GREEN FLUORESCENT PROTEINS; MUTATIONS; TRANSMEMBRANE SEGMENT M5;

CELLS;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; AMINO ACID; GLUTAMIC ACID; GLUTAMINE; PHOSPHORUS 32; POTASSIUM ION; SODIUM ION; THREONINE; VALINE; 4 NITROPHENYLPHOSPHATASE; CATION; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; OUABAIN; OXYGEN; POTASSIUM; SODIUM; SODIUM CHLORIDE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONCENTRATION RESPONSE; ENZYME ACTIVITY; HELA CELL; HUMAN; HUMAN CELL; ION TRANSPORT; MEMBRANE VESICLE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SODIUM TRANSPORT; AMINO ACID SEQUENCE; ANIMAL; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; GENETIC TRANSFECTION; KINETICS; LIPID BILAYER; METABOLISM; MOLECULAR GENETICS; MUTATION; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; RAT; SEQUENCE HOMOLOGY;

STROPHANTHUS GRATUS;

4-NITROPHENYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATIONS; CELL MEMBRANE; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUTAMIC ACID; GLUTAMINE; GREEN FLUORESCENT PROTEINS; HELA CELLS; HUMANS; KINETICS; LIPID BILAYERS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; OXYGEN; PHOSPHORYLATION; POTASSIUM; PROTEIN CONFORMATION; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM; SODIUM CHLORIDE; THREONINE; TRANSFECTION; VALINE;

EID: 21444457309     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M500137200     Document Type: Article

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