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. 2004 Aug 31;87(5):3181–3192. doi: 10.1529/biophysj.104.045559

TABLE 3.

Biophysical properties of E462R mutants with CaVβ2a wt and CS

Inactivation (5 s) E0.5 (mV)
Activation E0.5 (mV)
Peak IBa (μA)
With α2bδ in 10 Ba2+ +β2a +β2aCS +β2a +β2aCS +β2a +β2aCS
CEEE −18 ± 1 (5) z = 2.3 n.d. −4.6 ± 0.7 (2) z = 4.6 ± 0.3 −5.1 ± 0.6 (6) z = 3.8 ± 0.1 −0.51 ± 0.03 (2) −0.66 ± 0.06 (6)
CEEE + E462R −27.3 ± 0.5 mV (12) z = 2.5 −33.6 ± 0.7 mV (6) z = 2.6 −9.0 ± 0.4 (9) z = 5.0 ± 0.3 −5.7 ± .5 (14) z = 4.0 ± 0.2 −4.6 ± 0.9 (9) −1.6 ± 0.2 (14)
CaV1.2 (XhoI) wt n.d. n.d. −8.8 ± 0.6 (8) z = 3.9 ± 0.3 −5.9 ± 0.7 (4) z = 3.7 ± 0.2 −0.8 ± 0.1 (8) −0.58 ± 0.05 (4)
CaV1.2 E462R n.d. n.d. −11 ± 1 (8) z = 4.2 ± 0.3 −7.7 ± 0.9 (7) z = 4.9 ± 0.6 −0.9 ± 0.2 (8) −0.63 ± 0.08 (7)

Biophysical parameters of CaV1.2 and CEEE mutants expressed in Xenopus oocytes in the presence of CaVα2bδ and CaVβ2a or CaVβ2a C3S + C4S subunits. Whole-cell currents were measured in 10 mM Ba2+ throughout. The voltage dependence of inactivation was determined from the peak currents measured at 0 mV after 5 s pulses from −100 to +50 mV. Relative currents were fitted to Boltzmann Eq. 1. Activation data were estimated from the mean I/V relationships and fitted to Boltzmann Eq. 2. Peak IBa was determined from I/V relationships for the corresponding experiments. The data are shown with the mean ± SE and the number n of samples appears in parentheses.

n.d., not determined.