TABLE 3.
NA enzyme kinetics properties of purified influenza A(H1N1)pdm09 viruses
Virus | Vmax (μM/min) | Vmax ratioa | Km (μM)b | Kcat/Km (μM min)−1c |
---|---|---|---|---|
WT | 5.2 ± 0.7 | 1.0 | 203.7 ± 71.4 | 7.7 ± 2.8 |
LAN+IFN (P10) | 1.1 ± 0.8c | 0.2c | 7,666.0 ± 843.2c | 0.1 ± 0.04c |
The Vmax was calculated using nonlinear regression of the curve according to the Michaelis-Menten equation, and then the ratio of the respective viruses’ NA Vmax to the Vmax of the wild-type CA virus was determined.
The Km represents the Michaelis-Menten constant at which the reaction rate is half of Vmax. The enzyme kinetic data were fit to the Michaelis-Menten equation using GraphPad Prism, version 7.0. Values are the means ± 95% confidence interval from 3 independent determinations.
P < 0.05 compared with the value for WT by unpaired t test.