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. Author manuscript; available in PMC: 2014 Oct 17.
Published in final edited form as: Biochemistry. 2008 Sep 18;47(41):10940–10949. doi: 10.1021/bi801010u

Table 3.

Inhibition by µ-SIIIA of cloned sodium channels expressed in Xenopus oocytes. Rate constants were determined as described under Experimental. Standard deviation and 95% confidence intervals (95% C.I) were calculated from at least three independent experiments using Prism software.

Sodium
channela
kon
(µM−1.min−1)
koff
(min−1)
IC50(95% C.I.)
(µM)
rNaV1.1 0.011 ± 0.004 0.2 ± 0.06 11 (9.3–12.6)
rNaV1.2 0.10 ± 0.015 Irreversibleb N.A.c
rNaV1.3 0.017 ± 0.002 0.12 ± 0.018 11 (9.0–12.9)
rNaV1.4 0.29 ± 0.036 0.04 ± 0.008 0.13 (0.11–0.16)
rNaV1.5 --d --d 251 (204–308)e
mNaV1.6 0.06 ± 0.012 0.082 ± 0.006 0.76 (0.69–0.85)
rNaV1.7 0.005 ± 0.0005 0.075 ± 0.012 65 (57.8–73.1)
a

α-Subunit cloned from rat (r) or mouse (m).

b

Although the block was essentially irreversible within the experimental time frame, the koff was estimated as 0.0047 ± 0.0015 min−1 based on residual recovery after 20 min of wash and assuming exponential decay.

c

Not available because slow kinetics precluded steady state from being achieved within the experimental time frame.

d

Unable to be determined because block was too small and apparent kinetics too fast to be measured accurately.

e

Extrapolated value assuming 100% block at saturating peptide concentration.