cobalt has been researched along with magnesium phosphate (2:3) in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Buxbaum, E; Schoner, W | 2 |
2 other study(ies) available for cobalt and magnesium phosphate (2:3)
| Article | Year |
|---|---|
Blocking of Na+/K+ transport by the MgPO4 complex analogue Co(NH3)4PO4 leaves the Na+/Na(+)-exchange reaction of the sodium pump unaltered and shifts its high-affinity ATP-binding site to a Na(+)-like form.
Topics: 4-Nitrophenylphosphatase; Adenosine Triphosphate; Animals; Biological Transport, Active; Cobalt; Eosine Yellowish-(YS); Erythrocyte Membrane; Humans; Kidney; Magnesium; Magnesium Compounds; Ouabain; Phosphates; Quaternary Ammonium Compounds; Receptors, Purinergic; Sodium; Sodium-Potassium-Exchanging ATPase; Swine | 1990 |
Phosphate binding and ATP-binding sites coexist in Na+/K(+)-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4.
Topics: Adenosine Triphosphate; Animals; Binding Sites; Binding, Competitive; Cobalt; Enzyme Activation; Enzyme Stability; Kidney Medulla; Kinetics; Magnesium; Magnesium Compounds; Models, Biological; Phosphates; Potassium Chloride; Protein Conformation; Quaternary Ammonium Compounds; Sodium Chloride; Sodium-Potassium-Exchanging ATPase; Swine | 1991 |