Saturation binding of 125I-hCAL and 125I-AC512 to membranes from HEK 293 cells expressing hCTR2
| Cell Type | 125I-hCAL | 125I-AC512 | ||
|---|---|---|---|---|
| pKd1-a 95% c.i.1-b | Bmax1-c 95% c.i. | pKd1-a 95% c.i.1-b | Bmax1-d 95% c.i. | |
| Wild-type | 10.77 | 1.0 | 10.21 | 28.7 |
| 10.63 to 10.91 | 0.81 to 1.19 | 10.18 to 10.24 | 27.9 to 29.5 | |
| Gαi-enriched | 10.76 | 1.02 | 10.13 | 28.8 |
| 10.6 to 10.93 | 0.8 to 1.25 | 10.08 to 10.16 | 27.8 to 29.8 | |
| Gαs-enriched | 10.69 | 0.92 | 9.95 | 13.3 |
| 10.6 to 10.78 | 0.8 to 1.03 | 9.91 to 9.99 | 12.84 to 13.8 | |
| Gαo-enriched | 10.03 | 1.96 | 10.31 | 10.5 |
| 9.83 to 10.23 | 1.2 to 2.72 | 10.22 to 10.4 | 9.27 to 10.81 | |
| Gαq-enriched | 10.05 | 0.26 | 9.76 | 5.08 |
| 9.84 to 10.27 | 0.63 to 0.92 | 9.52 to 10.01 | 3.78 to 6.38 | |
↵1-a Log equilibrium dissociation constant of the 125I-hCAL/hCTR2 complex for high-affinity binding.
↵1-b 95% confidence limits of the estimate. Estimates are the mean of three separate transient transfections.
↵1-c Number of high affinity binding sites (picomoles per milligram of protein) as estimated with the RADLIG program. Although an estimate was made of the number of low-affinity binding sites, there were insufficient datapoints to allow a meaningful maximal asymptote to be measured.
↵1-d Estimate of the maximal number of binding sites for the antagonist radioligand 125I-AC512.