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Kinetic parameters of ATP and ADP dephosphorylation by NSAP on primary cultures of HBE cells
Michaelis constants (Km; μm) and maximal velocities (Vmax: nmol·min−1·ml−1) were calculated from Woolf-Augustinson Hoftsee plots.
| Reactions | Enzyme identity | Parameters | Experimental data |
|---|---|---|---|
| ATP → ADP + Pi | HighNSAP | Vmax, Km | 1.0, 17 |
| LowNSAP | Vmax, Km | 14.1, 451 | |
| ADP → AMP + Pi | HighNSAP | Vmax, Km | 0.5, 11 |
| LowNSAP | Vmax, Km | 5.9, 117 |
