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. 1997 Sep 15;17(18):6884–6891. doi: 10.1523/JNEUROSCI.17-18-06884.1997

Table 1.

Differential effects of α2δ and δ on the biophysical and binding properties of the α1C currents

Properties α1C α1C2δ α1C
Peak current amplitude (pA) −72  ± 15 −221  ± 24 −65  ± 11
Apparent activation threshold (mV) ≥−10 ≥−20 ≥−20
Potential for half-activation (mV) 19.6 8.7 8.5
Potential for half steady-state inactivation (mV) −6.8 −15.9 −16.4
Decay of the current at 150 msec* (%) 19.5  ± 4.2 39.2  ± 9.8 36.4  ± 6.2
Rate of inactivation at +20 mV (μsec−1) 2.5  ± 0.5 4.3  ± 0.4 4.6  ± 0.7
Bmax (fmol/mg of protein) 67  ± 29 141  ± 39 41  ± 10
KD(nm) 0.9  ± 0.5 0.1  ± 0.04 2.4  ± 0.9
*

 Currents were recorded during depolarizations from −80 to +30 mV.

Bmax, Maximum binding capacity;KD, dissociation constant (mean ± SE; n = 3–5).