Table 1.
No treatment | 10 nm ET-1 | 100 nm PMA | 10 nm Iso | ||
---|---|---|---|---|---|
Wild-type | Maximum ATPase rate | 207 ± 16 | 190 ± 26 | 175 ± 17* | 286 ± 12* |
Difference | — | n.s. | −16% | +38% | |
Maximum tension | 14.5 ± 1.1 | 12.8 ± 0.9 | 14.6 ± 1.6 | 12.7 ± 1.1 | |
Difference | — | n.s. | n.s. | n.s. | |
Ala2nb | Maximum ATPase rate | 197 ± 10 | 148 ± 15* | 149 ± 15* | 192 ± 18 |
Difference | — | −25% | −24% | n.s. | |
Maximum tension | 15.1 ± 1.3 | 14.0 ± 1.3 | 15.1 ± 1.2 | 13.8 ± 1.2 | |
Difference | — | n.s. | n.s. | n.s. | |
Ala5nb | Maximum ATPase rate | 176 ± 11 | 168 ± 9 | 165 ± 13 | 172 ± 17 |
Difference | — | n.s. | n.s. | n.s. | |
Maximum tension | 12.5 ± 1.2 | 13.3 ± 0.8 | 13.0 ± 1.5 | 13.5 ± 1.3 | |
Difference | — | n.s. | n.s. | n.s. |
Maximum MgATPase in units of (nmol Pi) min−1 (mg protein)−1 measured at pCa 4. Maximum active tension (total minus resting) in units of μm mm−2. Resting tension values were: 1.5 ± 0.2 (all wild-type), 1.6 ± 0.3 (all Ala2) and 1.8 ± 0.3 (all Ala5) in mm mm−2.
P < 0.05; n.s. = not significant; Data from a minimum of six separate experiments are reported as mean ±s.e.m.