Kd | nH | n | Reference | |
---|---|---|---|---|
nM | ||||
1, InsP3 | 3.09 ± 0.33 | 1.05 ± 0.08 | 24 | |
2, Adenophostin A | 0.48 ± 0.06 | 1.29 ± 0.10 | 10 | |
3, Purinophostin | 0.80 ± 0.25 | 1.12 ± 0.18 | 4 | Marwood et al., 2000b |
5, Imidophostin | 2.19 ± 0.80 | 1.06 ± 0.06 | 4 | Marwood et al., 2000b |
6, Ribophostin | 4.40 ± 0.80 | 0.99 ± 0.05 | 3 | |
12, manno -Adenophostin | 4.66 ± 0.62 | 0.83 ± 0.03 | 5 | |
13, Uridophostin | 1.20 ± 0.27 | 0.98 ± 0.07 | 3 | |
24, Furanophostin-PS2 | 39.5 ± 5.9 | 1.09 ± 0.14 | 4 |
The Kd and Hill coefficient (nH) determined from equilibrium competition binding with [3H]InsP3 are shown for selected ligands. To correct for variability between experiments performed over a substantial period, each binding assay was accompanied by a parallel measurement of InsP3 binding. For Fig. 7, the affinity of each analog was then expressed relative to that for InsP3 (see underExperimental Procedures). The data in this table show the results (from n independent experiments) before calibration to the relevant InsP3 affinity.