TABLE 1.
Kinetic properties of myosin-18A isoforms
KA and KTA were determined by hyperbolic fits to the binding data.
| Parameter | Signal or calculation | M. musculus MY018Aα | M. musculus MY018Aβ |
|---|---|---|---|
| ATP binding | |||
| KT (μm−1 s−1) | mantATP | 0.42 ± 0.03 | 0.12 ± 0.01 |
| k−T (s−1) | mantATPa | 7.29 ± 0.26 | 10.16 ± 0.09 |
| ADP interaction | |||
| k+D (μm−1 s−1) | mantADP | 0.17 ± 0.02 | 0.10 ± 0.02 |
| k−D (s−1) | mantADPb | 9.58 ± 0.15 | 10.87 ± 0.16 |
| mantADPc | 10.01 ± 0.23 | 10.3 ± 0.3 | |
| KD (μm) | k−D/k+D | 56.35 ± 6.69 | 108.70 ± 21.79 |
| Actin interaction | |||
| KA (μm) | Co-sedimentation | 5.9 ± 1.7 | 47.9 ± 9.2 |
| KTA (μm) | Co-sedimentationd | 4.9 ± 1.6 | 54.0 ± 29 |
a Ordinate of the kobs versus [mantATP] plot.
b Ordinate of the kobs versus [mantADP] plot.
c ATP chasing experiment.
d In the presence of 1 mm ATP.