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. 2012 Jun 12;287(31):25696–25705. doi: 10.1074/jbc.M112.373498

TABLE 3.

The parameters of force production and Pi release

Summary of results from length change experiments in the presence and absence of a creatine phosphate-creatine phosphokinase ATP regenerating system. Data was analysed using the two-way analysis of variance, general linear model (Systat, Software Inc., San Jose, CA).

Without ATP regenerating system
With ATP regenerating system
32 μm Ca2+ 1 μm Ca2+ 32 μm Ca2+ 1 μm Ca2+
n 5 5 10 5
Isometric force (kN m−2) 49.8 ± 6.4 24.7 ± 4.7a 54.0 ± 6.1 36.0 ± 8.4a
t½ (ms) 58.2 ± 2.1 77.5 ± 11.7 65.3 ± 8.3 86.6 ± 12.5
Stiffness (kN m−2 μm−1) 490 ± 143 460 ± 162 325 ± 89 324 ± 93
Peak force at end of stretch (kN m−2) 84.3 ± 15.7 61.6 ± 12.9 80.0 ± 7.3 61.9 ± 15.2
Force enhancement after stretch (kN m−2) 71.7 ± 14.0 49.1 ± 6.7 69.4 ± 6.1 57.1 ± 11.9
Force at end of release (kN m−2) 10.9 ± 1.7 6.1 ± 2.4 14.5 ± 2.4 7.7 ± 2.5b
Isometric force after release (kN m−2) 36.3 ± 3.0 16.0 ± 4.8a 38.7 ± 3.9 27.2 ± 5.9b
t½, force redevelopment (ms) 86.1 ± 9.5 127.3 ± 10.8 83.8 ± 9.2 80.2 ± 15.8c

ATPase rate (s−1)
    n 5 5 4 3
    Initial (first turnover) 15.2 ± 1.3 14.4 ± 1.1 14.7 ± 1.4 14.8 ± 1.4
    Steady state (isometric) 8.23 ± 0.5 4.8 ± 0.9b 7.5 ± 0.4 5.5 ± 0.4b
    During stretch 1.0 ± 0.9 1.5 ± 0.9 1.4 ± 1.2 0.3 ± 0.6
    After stretch 4.7 ± 0.3 4.4 ± 0.5 4.5 ± 0.17 4.4 ± 0.5
    During release 10.9 ± 1.5 7.8 ± 1.1 7.6 ± 0.8d 11.0 ± 0.6d
    End isometric 7.8 ± 1.3 3.7 ± 1.1b 6.8 ± 1.0 4.8 ± 0.8b

a p < 0.01 difference between submaximal and maximal activation.

b p < 0.05 difference between submaximal and maximal activation.

c p < 0.05 difference with and without ATP regenerating system.

d Identifies a significant (p = 0.027) interaction effect of the two main factors (calcium level and ATP regeneration) on Pi release rate during the cross-bridge release phase, but there is not a clear mechanistic explanation for this minor interaction effect.