Table 2.
Transient kinetic parameters measured for the exon 7 chimeric S1 isoforms Values are mean ± S.D. based on a minimum of 3 preparations. K1k+2 is the second order rate constant for ATP-induced dissociation of acto-S1. KD and KAD are dissociation equilibrium constants determined by division of the dissociation rate constant by the association rate constant (e.g. K3 = k−3 / k+3). k−D and k−AD are the ADP dissociation rate constants in the absence and presence of actin, respectively. KAD / KD is the thermodynamic coupling constant describing the relationship between actin and ADP affinities 28.
S1 Isoform |
IFI† | IFI-7a | EMB† | EMB-7d | EMB- 7a/7d |
EMB- 7d/7a |
---|---|---|---|---|---|---|
K1k+2 (106 M−1 s−1) |
0.75 ± 0.08 | 0.33 ± 0.07 | 0.91 ± 0.13 | 0.64 ± 0.05 | 0.67 ± 0.18 | 0.66 ± 0.14 |
k−D (s−1) | 7.5 ± 1.3d | 4.7 ± 0.8c,d | 1.8 ± 0.4c | 4.3 ± 0.7c,d | 2.6± 0.04c,d | 6.1 ± 0.08d |
KD (μM)a | 7.5 | 4.7 | 1.8 | 4.3 | 2.6 | 6.1 |
KAD (μM) | 409 ± 26d | 239 ± 52c,d | 587 ± 48c | 596 ± 39c | 191 ± 59c,d | 220 ± 33c,d |
k−AD (s−1)b | 4090 | 2390 | 5870 | 5960 | 1910 | 2200 |
KAD / KD | 55 | 51 | 326 | 139 | 73 | 36 |
Data are estimated from k−D assuming an association rate constant of 106 M−1 s−1.
Data are estimated from KAD assuming an association rate constant of 107 M−1 s−1.
Data are from Miller et al. 11
p < 0.05 determined by Student's t-test as compared to IFI
p < 0.05 determined by Student's t-test as compared to EMB