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. 2005 May 27;89(2):1009–1019. doi: 10.1529/biophysj.105.060152

TABLE 2.

Inactivation rate constants in whole oocytes

Control
In 0.5 μM κ−PVIIA
Average ± SE Average ± SE
kono (μM−1s−1) 50.0 koni (μM−1s−1) 28.3 ± 7.5
koffo (s−1) 25.0 koffi (s−1) 14.0 ± 5.4
ki (s−1) 0.187 ± 0.013 kib (s−1) 0.234 ± 0.074
kr (s−1) 0.049 ± 0.0042 krb (s−1) 0.054 ± 0.016
Ki 0.26 ± 0.0082 Kib 0.37 ± 0.190
κ−PVIIA binding constants
Open channels
Inactivated channels
KDo (μM) 0.5 KDi (μM) 0.68 ± 0.35

Kinetic and rate constants that describe Scheme 1 applied to the TEVC relaxation curves as those shown in Fig. 3. Values are the average of four oocytes to which the relaxations in the presence and in the absence of toxin were compared. The strategy to do the fitting is described in Materials and Methods. Ki and Kib, the apparent inactivation equilibrium constants at 0 mV, were calculated from kr/ki and krb/kib, respectively, whereas KDo and KDi were calculated from koffo/kono and koffi/koni, respectively. A value of ΔΔG = +0.2 kcal/mol results from the change in binding energy of the toxin to inactivated channels relative to the binding to open channels.