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. 2013 Nov 4;110(47):E4557–E4566. doi: 10.1073/pnas.1319218110

Table 1.

V0.5 and z at 100 and 0 mM [Na+]o

V0.5, mV
Z
Mutant 100 Na+ 0 Na+ 100 Na+ 0 Na+
hSGLT1 −39 ± 2 < −120 1.0 ± 0.1 n.m.
Near sugar binding
 H83C −42 ± 3 −120 to −140 0.9 ± 0.1 n.m.
 T287C −47 ± 1 < −120 1.0 ± 0.1 n.m.
 Y290C 3 ± 4 −54 ± 4 0.9 ± 0.1 0.6 ± 0.1
 Y290S 18 ± 1 −40 ± 6 0.9 ± 0.1 0.7 ± 0.1
 Y290F −49 ± 13 < −120 0.9 ± 0.1 n.m.
 W291C 12 ± 2 −53 ± 2 0.9 ± 0.1 0.6 ± 0.1
 W291F −49 ± 9 < −120 1.0 ± 0.1 n.m.
 Q457C −55 ± 4 < −120 1.0 ± 0.1 n.m
Near Na2 site
 D204E* −50 ± 2 −67 ± 3 ∼1 ∼1
 S392A/C −56 ± 3 −100 to −140 0.9 ± 0.1 n.m.
Other
 F101C −3 ± 3 < −120 1.0 ± 0.1 n.m.
 F453C −28 ± 4 < −120 1.0 ± 0.1 n.m.
 G507C −35 ± 1 < −120 1.0 ± 0.1 n.m.

Kinetics are mean ± SE of three to nine oocytes from at least two donor frogs. For mutants with Q/V curves that did not saturate (within the range −150 mV and +50 mV) at 0 Na+, we were unable to obtain reliable estimates of V0.5 and z. V0.5 was more negative than −120 mV (< −120 mV) and z was designated by nonmeasurable (n.m.). At 0 Na+, z = z1, and at 100 mM Na+, z = z1 + z2 + z3 (Eq. 9).

*

Data are from Quick et al. (25), where the data at 0 Na+ were actually obtained in 5 mM Na+.