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. 2012 Sep 10;590(Pt 23):6047–6063. doi: 10.1113/jphysiol.2012.240085

Table 2.

Parameter estimates of muscle fibre contractile function

Fibres from normal mice (α-MHC) Fibres from PTU-treated mice (β-MHC)


α-MHC(cTnI) α-MHC(ssTnI) β-MHC(cTnI) β-MHC(ssTnI)
Max Tens 43.8 ± 1.53 48.0 ± 0.76a 52.8 ± 2.37a 47.7 ± 1.56
Max ATPase 320 ± 18.6 359 ± 24.2 146 ± 5.19a 169 ± 7.73b,c
E 595 ± 26.8 651 ± 19.1 749 ± 32.4a 705 ± 27.4
E0/E 0.32 ± 0.02 0.33 ± 0.01 0.27 ± 0.01a 0.30 ± 0.01
pCa50 5.78 ± 0.01 6.11 ± 0.01a 5.85 ± 0.01a 5.90 ± 0.01b,c
nH 2.16 ± 0.09 1.80 ± 0.04a 2.46 ± 0.06a 2.62 ± 0.05c

Maximal tension production (mN mm−2) and rate of ATPase activity (pmol mm−3 s−1) were measured from α-MHC and β-MHC NTG and ssTnI TG mice. E (mN mm−3) is the stiffness approximated at infinite frequency of chirp perturbation, and correlates with maximal tension production. E0/E (unitless) is an approximation of the magnitude of length-mediated XB recruitment as a fraction of the number of strongly bound XB prior to perturbation. Hill's equation was fitted to pCa–tension relationships (Fig. 7) to determine parameters for myofilament Ca2+ sensitivity, pCa50, and cooperativity, nH. Values are means ± SEM. Number of determinants is at least 10 for each group. aP < 0.05 vs. α-MHC(cTnI); bP < 0.05 vs. β-MHC(cTnI); cP < 0.05 vs. α-MHC(ssTnI).