Substitutions of glutamate 781 in the Na,K-ATPase α subunit demonstrate reduced cation selectivity and an increased affinity for ATP

Journal of Biological Chemistry

Volumn 271, Issue 5, 1996, Pages 2413-2421

  Koster, Joseph C ^a   Blanco, Gustavo ^a   Mills, Paul B ^a   Mercer, Robert W ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); OUABAIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBUNIT; GENE MUTATION; NONHUMAN; POTASSIUM TRANSPORT; PRIORITY JOURNAL; RAT; SODIUM TRANSPORT;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CESIUM; CLONING, MOLECULAR; GLUTAMIC ACID; HYDROLYSIS; ION TRANSPORT; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NA(+)-K(+)-EXCHANGING ATPASE; POTASSIUM; SODIUM; SPODOPTERA; TRYPSIN;

ANIMALIA; INSECTA; STROPHANTHUS GRATUS; UNIDENTIFIED BACULOVIRUS;

EID: 0030028519     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.5.2413     Document Type: Article

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