Table II.
Q10 Values for Ion Channel Permeation and Gating
| Channel | °C | Conductance | τact | τtail | τi | τrecovery | Reference | |||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| KIR (frog muscle) | 3.5–17.5 | 1.67 | 2.45 | — | — | — | Almers, 1971 | |||||||
| (tunicate oocyte) | 5–20 | 1.44* | — | — | 3.41V * | — | Ohmori, 1978 | |||||||
| (starfish oocyte) | 1–26 | 1.62H–5.8L | — | — | — | — | Hagiwara and Yoshii, 1980 | |||||||
| (guinea pig myocyte) | 5–37 | 1.15 | 1.45 | — | — | — | Martin et al., 1995 | |||||||
| (cat cardiac myocyte) | 5–37 | 1.22 | 1.82 | — | — | — | Martin et al., 1995 | |||||||
| KV (Xenopus laevis) | 5–20 | 1.2 | 3.2 | 2.8 | — | — | Frankenhaeuser and Moore, 1963 | |||||||
| (Myxicola axon) | 5–14 | — | 2.40 | — | 3.02β | 1.70β | Schauf and Bullock, 1982 | |||||||
| (rat muscle) | 1–37 | 1.42 | 2H–6L | 1.7H–11.5L | — | — | Beam and Donaldson, 1983 | |||||||
| (human T-cell) | 27–37 | 1.56 | 3.31 | 7.09 | 3.87 | 9.81 | Lee and Deutsch, 1990 | |||||||
| (human T-cell) | 20–25 | 1.18* | 2.9 | — | 2.2 | — | Pahapill and Schlichter, 1990 | |||||||
| ShB K+ peptide | 5–20 | — | — | — | 5.0176 | <1.1176 | Murrell-Lagnado and Aldrich, 1993 | |||||||
| Shaker K+ | 5–20 | 1.51 | 3.14 | — | 7.2 | 1.57 | Nobile et al., 1997 | |||||||
| KCa (human RBC) | 0–47 | 1.50 | — | — | — | — | Grygorczyk, 1987 | |||||||
| Na+ (X. laevis) | 5–20 | 1.3 | 1.8 | 1.7 | — | — | Frankenhaeuser and Moore, 1963 | |||||||
| (squid axon) | 0–16 | — | 2.35 | — | 2.7H–4.3L | — | Kimura and Meves, 1979 | |||||||
| (rabbit nerve) | 0–25 | 1.7H–4.7L | — | — | 3H–33L | — | Chiu et al., 1979 | |||||||
| (neuroblastoma) | 5.6–14 | — | — | — | 1.3α * | 1.3α * | Yamamoto and Yeh, 1984 | |||||||
| (frog muscle) | 0–22 | — | 2.4 | — | 3.0H–5.3L | — | Kirsch and Sykes, 1987 | |||||||
| (rabbit muscle) | 0–22 | — | 2.3 | — | 3.4H–9.1L | — | Kirsch and Sykes, 1987 | |||||||
| AchR (BC3H-1) | 10–40 | 1.26H–1.55L * | 3.6* | — | — | — | Dilger et al., 1991 | |||||||
| Ca2+ (muscle) | — | 1.3–1.6* | ∼3.0 | ∼3.0 | — | — | McDonald et al., 1994 | |||||||
| CIC-0 | 9–40 | 1.4* | — | 2.2 | ∼40 | — | Pusch et al., 1997 | |||||||
| Alamethicin | −1–32 | 1.28–1.31 | 2.9H–9.0L | 2.04 | — | — | Boheim and Kolb, 1978 | |||||||
| Gramicidin (K+, Na+) | 3–23 | 1.38,* 1.34* | — | 3.1* | — | — | Hladky and Haydon, 1972 | |||||||
| Gramicidin (Na+) | 10–40 | 1.52* | 3.09 | 2.62 | — | — | Bamberg and Läuger, 1974 | |||||||
| Gramicidin (H+) | 15–22 | 1.33* | — | — | — | — | Akeson and Deamer, 1991 | |||||||
| H+ (snail neuron) | 10–25 | 2.1 | — | — | — | — | Byerly and Suen, 1989 | |||||||
| (mammalian cells) | 5–44 | 2.8H, 5.3L | 6–9 | 6–8 | — | — | This study |
For a variety of ion channels, Q 10 values are listed for the conductance, and for kinetic parameters reflecting gating transitions: activation, deactivation, and inactivation (in some cases block). Q 10 values not given in original references were calculated from Arrhenius activation energy values or other available data (see materials and methods).
Values for single channel currents, which are not complicated by possible interactions between gating and conductance. Several measurements reflect block, rather than intrinsic gating: vvoltage-dependent Na+ block,
block by the inactivation peptide, βblock and unblock by nonyltriethylammonium ions, αblock and unblock by 9-aminoacridine. H Q 10 at higher temperatures, L Q 10 at lower temperatures.