Molecular distance measurements reveal an (αβ)2 dimeric structure of Na+/K+-ATPase: High affinity ATP binding site and K+-activated phosphatase reside on different α-subunits

Journal of Biological Chemistry

Volumn 273, Issue 44, 1998, Pages 28813-28821

  Linnertz, Holger ^a   Urbanova, Petra ^b   Obsil, Tomas ^b   Herman, Petr ^c   Amler, Evzen ^b   Schoner, Wilhelm ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^c CHARLES UNIVERSITY   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); PHOSPHATASE; PROTEIN SUBUNIT;

ARTICLE; BINDING AFFINITY; BINDING SITE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

ADENOSINE TRIPHOSPHATE; AFFINITY LABELS; ANIMALS; BINDING SITES; CATALYSIS; DIMERIZATION; ENZYME ACTIVATION; ERYTHROSINE; ISOTHIOCYANATES; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PHOSPHORIC MONOESTER HYDROLASES; POTASSIUM; SWINE;

EID: 0032582504     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.44.28813     Document Type: Article

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