Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. XV. Direct chemical characterization of the acyl phosphate in the enzyme as an aspartyl beta-phosphate residue.
Nishigaki, I
Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. XV. Direct chemical characterization of the acyl phosphate in the enzyme as an aspartyl beta-phosphate residue. [electronic resource] - The Journal of biological chemistry Aug 1974 - 4911-6 p. digital
Publication Type: Journal Article
0021-9258
Adenosine Triphosphatases--metabolism
Amino Acids--analysis
Animals
Aspartic Acid
Binding Sites
Biological Transport
Borohydrides
Hydrogen-Ion Concentration
Organophosphorus Compounds
Oxidation-Reduction
Phosphates--analysis
Phosphorus Radioisotopes
Potassium
Protein Binding
Sharks
Sodium
Spectrophotometry
Time Factors
Tritium
Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. XV. Direct chemical characterization of the acyl phosphate in the enzyme as an aspartyl beta-phosphate residue. [electronic resource] - The Journal of biological chemistry Aug 1974 - 4911-6 p. digital
Publication Type: Journal Article
0021-9258
Adenosine Triphosphatases--metabolism
Amino Acids--analysis
Animals
Aspartic Acid
Binding Sites
Biological Transport
Borohydrides
Hydrogen-Ion Concentration
Organophosphorus Compounds
Oxidation-Reduction
Phosphates--analysis
Phosphorus Radioisotopes
Potassium
Protein Binding
Sharks
Sodium
Spectrophotometry
Time Factors
Tritium