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. Author manuscript; available in PMC: 2008 May 11.
Published in final edited form as: J Mol Biol. 2007 Feb 22;368(4):1051–1066. doi: 10.1016/j.jmb.2007.02.042

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 = k3 / k+3). kD and kAD 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
kD (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
kAD (s−1)b 4090 2390 5870 5960 1910 2200
KAD / KD 55 51 326 139 73 36
a

Data are estimated from kD assuming an association rate constant of 106 M−1 s−1.

b

Data are estimated from KAD assuming an association rate constant of 107 M−1 s−1.

Data are from Miller et al. 11

c

p < 0.05 determined by Student's t-test as compared to IFI

d

p < 0.05 determined by Student's t-test as compared to EMB

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