Identification of Potential Regulatory Sites of the Na+,K +-ATPase by Kinetic Analysis

Biochemistry

Volumn 43, Issue 8, 2004, Pages 2241-2250

  Kong, Benjamin Y ^a   Clarke, Ronald J ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; DISSOCIATION; MATHEMATICAL MODELS; PHYSIOLOGY; RATE CONSTANTS;

BINDING STEPS; STEADY-STATE ACTIVITY;

ENZYME KINETICS;

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

ARTICLE; BINDING SITE; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME METABOLISM; EQUILIBRIUM CONSTANT; KINETICS; MATHEMATICAL MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PHOSPHORYLATION; STEADY STATE;

ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CATIONS, MONOVALENT; CATTLE; COMPUTER SIMULATION; ENZYME ACTIVATION; EXTRACELLULAR SPACE; INTRACELLULAR FLUID; KINETICS; MALE; MODELS, CHEMICAL; NA(+)-K(+)-EXCHANGING ATPASE; PHOSPHORYLATION; POTASSIUM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RABBITS; SODIUM;

HUMAN ECHOVIRUS 1;

EID: 1442300951     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0355443     Document Type: Article

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