TABLE 1.
Equilibrium Kd and Rt values for B. thuringiensis crystal proteins for BBMV of susceptible strain LAB-V of P. xylostella obtained with different 125I-labeled ICPs
| 125I-labeled ICP | Binding characteristics of ICPsa
|
|||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Cry1Aa
|
Cry1Ab
|
Cry1Ac
|
Cry1F
|
|||||||
| Kd1 (nM) | Rt1 (pmol/mg of protein)b | Kd2 (nM) | Rt2 (pmol/mg of protein)b | Kd (nM) | Rt (pmol/mg of protein)b | Kd (nM) | Rt (pmol/mg of protein)b | Kd (nM) | Rt (pmol/mg of protein)b | |
| Cry1Aa | 0.1 ± 0.1 | 0.2 ± 0.2 | 17.7 ± 1.0 | 6.2 ± 0.1 | 0.8 ± 0.2 | 2.7 ± 0.4 | 0.6 ± 0.2 | 2.0 ± 0.3 | ||
| Cry1Ab | 27.0 ± 5.7 | 0.3 ± 0.1 | 0.4 ± 0.2 | 0.3 ± 0.1 | 5.5 ± 2.0 | 0.8 ± 0.4 | ||||
| Cry1Ac | 17.2 ± 2.8 | 2.3 ± 0.6 | 5.0 ± 0.4 | 1.3 ± 0.1 | 17.0 ± 0.2 | 1.0 ± 0.1 | 13.0 ± 1.0 | 2.0 ± 0.1 | ||
a
Values are means ± standard deviations for four experiments performed with two independently prepared batches of BBMV for labeled Cry1Aa and for two experiments performed with the same batch of BBMV for the other labeled ICPs.
b
Picomoles per milligram of vesicle protein.