000 01408 a2200421 4500
005 20250512100129.0
264 0 _c19741002
008 197410s 0 0 eng d
022 _a0021-9258
040 _aNLM
_beng
_cNLM
100 1 _aNishigaki, I
245 0 0 _aStudies 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.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cAug 1974
300 _a4911-6 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAdenosine Triphosphatases
_xmetabolism
650 0 4 _aAmino Acids
_xanalysis
650 0 4 _aAnimals
650 0 4 _aAspartic Acid
650 0 4 _aBinding Sites
650 0 4 _aBiological Transport
650 0 4 _aBorohydrides
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aOrganophosphorus Compounds
650 0 4 _aOxidation-Reduction
650 0 4 _aPhosphates
_xanalysis
650 0 4 _aPhosphorus Radioisotopes
650 0 4 _aPotassium
650 0 4 _aProtein Binding
650 0 4 _aSharks
650 0 4 _aSodium
650 0 4 _aSpectrophotometry
650 0 4 _aTime Factors
650 0 4 _aTritium
700 1 _aChen, F T
700 1 _aHokin, L E
773 0 _tThe Journal of biological chemistry
_gvol. 249
_gno. 15
_gp. 4911-6
999 _c4282055
_d4282055