Table 4.
Binding affinities of rGmolPBPs and rGmolGOBPs for Z8-14:Ac.
| Protein Name | Kd (μM) | IC50 (μM) | Ki (μM) |
|---|---|---|---|
| GmolPBP1 | 1.29 ± 0.02 | 2.93 ± 0.07 | 1.66 ± 0.04 c |
| GmolPBP2 | 1.09 ± 0.02 | 1.26 ± 0.04 | 0.66 ± 0.02 d |
| GmolPBP3 | 11.24 ± 0.08 | 2.78 ± 0.32 | 2.56 ± 0.27 b |
| GmolGOBP1 | 5.76 ± 0.01 | >14 | >14 a |
| GmolGOBP2 | 4.32 ± 0.02 | 3.53 ± 0.22 | 2.86 ± 0.18 b |
Note: IC50: the concentration of Z8-14:Ac when replacing 1−NPN to reduce the initial fluorescence intensity of the rGmolPBP(rGmolGOBP)/1−NPN complex to 50%; Kd: the dissociation constants of each rGmolPBP (rGmolGOBP) binding to 1−NPN; Ki: the inhibition constants of Z8-14:Ac competitive binding with each GmolPBP (GmolGOBP) from the protein/1−NPN complex. Data in the table are presented as mean ± SE (n = 3). Different lowercase letters after the data in the same column indicate significant differences in the affinities of different recombinant proteins for binding to Z8-14:Ac (p < 0.05, one-way ANOVA followed by Tukey’s HSD test).