Table 2.
EC50 (nM) | Number | p | Fold shifta | Emax (% ± SEM) | p | |
---|---|---|---|---|---|---|
wt | 605 ± 79 | 5 | 136 ± 12 | |||
F110A | 44 ± 8 | 3 | ** | 14 | 129 ± 9 | ns |
N115A | 166 ± 52 | 4 | ** | 4 | 124 ± 11 | ns |
N173A | 131 ± 2 | 3 | ** | 5 | 146 ± 8 | ns |
F179A | 82 ± 15 | 3 | ** | 7 | 141 ± 6 | ns |
N194A | Very minor effect | 5 | nd | |||
F195A | 107 ± 10 | 3 | ** | 6 | 174 ± 12 | ns |
L201A | No effect | 4 | nd | |||
H252A | 718 ± 132 | 3 | ns | 1 | 146 ± 15 | ns |
Y268A | 7,082 ± 1,220 | 4 | *** | 0.08 | 229 ± 20 | * |
Number, number of experiments performed in triplicates; nd not determined; Emax value, maximal effect of the specific binding of [35S]GTPγS; binding in the absence of adenine was set at 100 %; p, significance was determined using the unpaired t test, mutants were compared to rAdeR coexpressed with G proteins; ns not significant
p > 0.05; *p < 0.05; **p < 0.01; ***p < 0.001
aThe shift represents the ratio of EC50 (wt)/EC50 (mutant)