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J. Gen. Physiol.,
Volume 112 October 1998 523-523
Jones, L.P., S.-k. Wei, and D.T. Yue. The Journal of General Physiology. Volume 112, No. 2, August 1998. 125-143.
Page 137.
Line five of Figure 9 legend contained an error in which two symbols were incorrectly labelled. The correct legend is shown below.
FIGURE 9. Activation and inactivation properties of a COOH-terminal truncated version of
1E (
1E
, amino acids 1-1871) that lacks a putative
binding site. All measurements for both
1E and
1E
are in 10 mM Ba2+. (A) Traces illustrating activation of ionic currents for
1E
2
(cell 375_19) or
1E
2a
2
(cell 370_6) using the same voltage protocol as in Fig. 2. Data are shown for test pulse potentials of
30,
20,
10, 10, and 50 mV. (B) Comparison of G-V for
1E
and
1E indicates that modulation of
1E
activation by
subunits is preserved. Symbols correspond to data for
1E
and wild-type
1E (
1E
2a
2
,
, n = 4;
1E
2
,
, n = 11;
1E
2
,
, n = 11; and
1E
2a,
, n = 8). Lines are single-Boltzmann fits to the
1E
2 and
1E
2a data with fit parameters z = 2.4, V1/2 =
10.1; and z = 3.4, V1/2 =
18.2,
respectively. The shift in V1/2 values relative to Fig. 6 C corresponds to a surface potential shift between 10 mM (used here) and 2 mM Ba2+
(Fig. 6). (C) Steady state inactivation. Traces after a 20-s prepulse (as in Fig. 7) to the indicated potentials are shown for
1E
in combination with
2
(cell 376_9),
3 (cell 375_4),
2a
2
(cell 370_11), and
3
2
(cell 371_10). (D) Comparison of h(
)-V relations for
1E
(symbols) and
1E (same data as in Fig. 7, shown as lines connecting mean data values, without explicit reproduction of data points as symbols).
Symbols correspond to the following constructs:
1E
2
,
;
1E
2a
2
,
;
1E
3,
;
1E
3
2
, ×. Data for
1E is shifted by
7 mV to
overlay the
1E
data. Average fit values and cell numbers are summarized in Tables V (G-V) and III [h(
)-V] for both
1E and
1E
.
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