Isoform-specific interactions of Na,K-ATPase subunits are mediated via extracellular domains and carbohydrates

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 4, 1997, Pages 1136-1141

  Schmalzing, Günther ^a   Ruhl, Karina ^a   Gloor, Sergio M ^b  

^a GOETHE UNIVERSITY   (Germany)

^b ETH ZURICH   (Switzerland)

Author keywords

assembly; detergents; K pump isozymes; N glycosylation; Na

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); DETERGENT; GLYCAN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; CONFORMATION; GENE EXPRESSION REGULATION; IMMUNOPRECIPITATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN INTERACTION; XENOPUS LAEVIS;

ANIMALS; CELL POLARITY; ENZYME INHIBITORS; ENZYME STABILITY; GLYCOPROTEINS; ISOENZYMES; MICE; MODELS, MOLECULAR; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PROTEIN BINDING; PROTEIN CONFORMATION; RATS;

ANIMALIA; RODENTIA; STROPHANTHUS GRATUS; XENOPUS LAEVIS;

EID: 0031029915     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.4.1136     Document Type: Article

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