TABLE 2 .
The surface plasmon resonance kinetics for binding of aldolase to the cytoplasmic tails of TRAP, RH1, RH2b, RH4, and GAPDH compared to that of BAEBLa
| Analyte (bridging molecule) |
Ligand (peptide) |
ka1 (M−1 S−1) |
kd1 (s−1) |
ka2 (s−1) |
kd2 (s−1) |
KD (nM) |
|---|---|---|---|---|---|---|
| Aldolase | TRAP | 3.37E+4 | 0.052 | 0.007 | 5.12E-4 | 106 |
| RH1 | 4.54E+4 | 0.082 | 0.018 | 6.47E-4 | 61 | |
| RH2b | 855.8 | 1.83E-4 | 214 | |||
| RH4 | 1.60E+4 | 0.034 | 0.012 | 2.69E-4 | 47 | |
| GAPDH | BAEBL | 1.02E+4 | 0.016 | 0.008 | 0.003 | 461 |
a
Kinetic parameters of the rabbit muscle aldolase and GAPDH binding to different peptides were obtained by fitting the concentration-dependent sensorgrams to 1:1 for RH2B or a two-state model for the other peptides. ka and kd are association and dissociation rate constants, respectively, and KD is the binding affinity (in nanomoles) obtained using the following equations: KD = ka/kd (for 1:1 kinetics) and KD = (ka1/kd1) × (ka2/kd2) (for two-state kinetics). TRAP, Thrombospondin Related Anonymous Protein. RH, reticulocyte homology. M−1 s−1, 1/mole/second.