Calorimetry of Na,K-ATPase

Annals of the New York Academy of Sciences

Volumn 986, Issue , 2003, Pages 245-246

  Stolz, M ^a   Lewitzki, E ^a   Schick, E ^a   Mutz, M ^b   Grell, E ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Calorimetry; DSC; ITC; Nucleotide binding; Ouabain binding; Thermal denaturation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM); ADENOSINE TRIPHOSPHATE;

BINDING AFFINITY; CALORIMETRY; CONFERENCE PAPER; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; PROTEIN BINDING; PROTEIN INTERACTION; STOICHIOMETRY; TITRIMETRY;

STROPHANTHUS GRATUS;

EID: 0038240785     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb07172.x     Document Type: Conference Paper

References (4)

1. GRELL, E., E. SCHICK & E. LEWITZKI. 2001. Membrane receptor calorimetry: cardiac glycoside interaction with Na,K-ATPase. Thermochim. Acta 380: 245-254.
2. +-ATPase as the cardiac glycoside receptor: a thermochemical characterization. J. Therm. Anal. 49: 1-9.
3. +-exchanging ATPase. Eur. J. Biochem. 268: 5027-5036.
4. FEDOSOVA, N., P. CHAMPEIL & M. ESMANN. 2002. Nucleotide binding to Na,K-ATPase: the role of electrostatic interactions. Biochemistry 41: 1267-1273 (and citations herein).