Table 1.
[ATP] |
d, nm |
ton, ms
|
||
---|---|---|---|---|
pH 7.4 | pH 6.4 | pH 7.4 | pH 6.4 | |
0.5 μM | N/A | 2±2 | N/A | 200±114 |
1 μM | 10±2 | 2±1* | 178±67 | 119±22 |
10 μM | 11±2 | 6±5 | 21±31 | 70±31* |
1 mM | 10† | 9±3 | 10† | 31±9 |
The values displayed, obtained by mean variance analysis, are the means ± SD from 4 to 10 single molecule data records, each 1–3 min in length, containing hundreds of events. d, unitary step size of myosin; ton, strong binding variable; N/A, not applicable.
Extrapolated or estimated value from Baker et al. (3).
Significantly different (P < 0.05) from the value at the corresponding [ATP] at pH 7.4. The data were analyzed using a two-way ANOVA (pH × ATP) with a Tukey-HSD post hoc test to locate specific differences. A subset of data using smooth muscle myosin at 1 mM ATP showed that d was unaffected by low pH (9 nm at pH 7.4 vs. 9 nm at pH 6.4), whereas ton was threefold longer (27 ms at pH 7.4 vs. 100 ms at pH 6.4), consistent with the observations in skeletal myosin.