The β subunit of the Na+/K+-ATPase follows the conformational state of the holoenzyme

Journal of General Physiology

Volumn 125, Issue 5, 2005, Pages 505-520

  Dempski, Robert E ^a   Friedrich, Thomas ^a,b   Bamberg, Ernst ^a,b  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b GOETHE UNIVERSITY   (Germany)

Author keywords

Conformational change; Electrogenic steps; Kinetics; Subunit interaction; Voltage clamp fluorometry

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); AMINO ACID; CATION; CYSTEINE; FLUORESCENT DYE; HOLOENZYME; ISOPROTEIN; LYSINE; MALEIMIDE DERIVATIVE; PROTEIN SUBUNIT; TETRAMETHYLRHODAMINE 6 MALEIMIDE; TETRAMETHYLRHODAMINE ETHYL ESTER; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BETA CHAIN; CATALYSIS; CATION TRANSPORT; CELL MEMBRANE POTENTIAL; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME CONFORMATION; ENZYME STRUCTURE; FLUOROMETRY; ION TRANSPORT; KINETICS; NONHUMAN; OOCYTE; PROTEIN HYDROLYSIS; SHEEP; SIGNAL TRANSDUCTION; SODIUM TRANSPORT; VOLTAGE CLAMP; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELLS, CULTURED; FEMALE; FLUORESCENCE; KINETICS; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS; NA(+)-K(+)-EXCHANGING ATPASE; OOCYTES; PATCH-CLAMP TECHNIQUES; POTASSIUM; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SHEEP; SODIUM; XENOPUS LAEVIS;

EID: 18544383760     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200409186     Document Type: Article

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