Half-site modification of Lys-480 of the Na+,K+-ATPase α-chain with pyridoxal 5'-diphospho-5'-adenosine reduces ATP-dependent phosphorylation stoichiometry from half to a quarter

Journal of Biological Chemistry

Volumn 273, Issue 38, 1998, Pages 24334-24338

  Tsuda, Takeo ^a   Kaya, Shunji ^a   Yokoyama, Takeshi ^a   Hayashi, Yutaro ^b   Taniguchi, Kazuya ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b KYORIN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID DERIVATIVE; ACETYL PHOSPHATE; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE PYRIDOXAL; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; ASPARTIC ACID; FLUORESCEIN ISOTHIOCYANATE; KIDNEY ENZYME; LYSINE; MAGNESIUM; OLIGOMYCIN; PYRIDOXINE DERIVATIVE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ALPHA CHAIN; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DOG; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; STOICHIOMETRY; SWINE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AFFINITY LABELS; ANIMALS; DOGS; KIDNEY; KINETICS; LYSINE; MACROMOLECULAR SUBSTANCES; MAGNESIUM; MODELS, STRUCTURAL; NA(+)-K(+)-EXCHANGING ATPASE; PHOSPHORYLATION; PYRIDOXAL PHOSPHATE; SODIUM; SWINE; TIME FACTORS;

ANIMALIA; CANIS FAMILIARIS; SUS SCROFA;

EID: 0032544352     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.38.24334     Document Type: Article

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