Ouabain and substrate affinities of human Na+-K+-ATPase α1β1, α2β1 and α3β1 when expressed separately in yeast cells

American Journal of Physiology - Cell Physiology

Volumn 281, Issue 4 50-4, 2001, Pages

  Müller Ehmsen, Jochen ^a,c   Juvvadi, Padmaja ^a   Thompson, Curtis B ^a   Tumyan, Lusine ^a   Croyle, Michelle ^b   Lingrel, Jerry B ^b   Schwinger, Robert H G ^c   McDonough, Alicia A ^a   Farley, Robert A ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Cardiac glycosides; Heterologous expression; Sodium pump

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; CARDIAC GLYCOSIDE; DIMER; ISOENZYME; OUABAIN; POTASSIUM ION; SODIUM ION;

ARTICLE; BINDING AFFINITY; DISSOCIATION CONSTANT; ENZYME BINDING; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; GENE EXPRESSION; GENE EXPRESSION SYSTEM; HUMAN; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; YEAST CELL;

EID: 0034796450     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.2001.281.4.c1355     Document Type: Article

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