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 |