Table 1.
Biochemical properties of different BBP-A forms.
| Gel filtration | SDS-PAGE-based thermostability assay | Dissociation of fluorescent BTN (25°C) | DSC | |||||||
| Elution time (min) | Molecular mass (kDa)a | Tr (°C) | kdiss (10-5 s-1) | Release 1 h (%) | Tm (°C) | |||||
| -BTN | +BTN | -BTN | +BTN | -BTN | +BTN | -BTN | +BTN | |||
| bBBP-A | 29.9 | 30.1 | 42.7 | 40.9 | N. D. | 70 | 54.8 | 86 | N. A. | 103.4 |
| bBBP-A (A74S) | 30.0 | 30.1 | 41.9 | 40.8 | N. D. | 75 | 47.1 | 83 | N. A. | 103.2 |
| bBBP-A (T118F) | 30.1 | 29.9 | 41.3 | 42.7 | N. D. | 70 | 69.1 | 94 | N. A. | 102.3 |
| iBBP-A | 28.4 | 28.4 | 60.8 | 59.7 | N. D. | 75 | 20.4 | 53 | N. M. | N. M. |
| AVD | 28.2 | 28.2 | 62.5 | 63.6 | 60b | 90b | 2.0 | 10 | 83.5c | 117.0 |
| bAVD | 28.8 | 28.8 | 55.3 | 55.1 | 60b | 90b | 1.1 | 5 | N. M. | N. M. |
N. D. Protein appeared mainly in monomeric form already at room temperature; N. A. Not applicable; N. M. Not measured.
aMolecular mass calculated from the measured elution times of thyroglobulin (670 kDa), gamma-globulin (158 kDa), BSA (67 kDa), ovalbumin (44 kDa) and myoglobin (17 kDa).
bResults from ref. [30].
cResults from ref. [33].