Binding of 1 Rb+ accelerates dephosphorylation of the Na+,K+-ATPase without leading to Rb+ occlusion

Annals of the New York Academy of Sciences

Volumn 986, Issue , 2003, Pages 155-158

  Kaufman, Sergio B ^a   González Lebrero, Rodolfo M ^a   Garrahan, Patricio J ^a   Rossi, Rolando C ^a  

^a UNIVERSIDAD DE BUENOS AIRES   (Argentina)

Author keywords

Dephosphorylation; Kinetics; Occlusion

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); POTASSIUM ION; RUBIDIUM ION;

BINDING AFFINITY; CONFERENCE PAPER; DEPHOSPHORYLATION; ENZYME ACTIVITY; STEADY STATE;

EID: 0038240818     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb07153.x     Document Type: Conference Paper

References (4)

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2. JENSEN J., J.G. NØRBY & P. OTTOLENGHI. 1984. Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour. J. Physiol. (London) 346: 219-241.
3. +-ATPase in steady state. Biochim. Biophys. Acta 1233: 33-40.
4. ROSSI, R.C. et al. 1999. An attachment for non-destructive, fast quenching of samples in rapid mixing experiments. Anal. Biochem. 270: 276-285.