Table 1.
The oligomeric state of β1a constructs
The oligomeric state of β1a constructs in solution was calculated by dividing the observed weight-averaged molecular mass with that of the theoretical monomer. Molecular masses greater than 1 MDa eluted close to the void volume of the gel-filtration column and furthermore cannot be accurately determined by MALS; thus they have been designated as “aggregated” protein. Errors in the calculation of observed molecular mass are given. The average protein concentration (μm) corresponding to each peak at the detector is given.
| Protein | Molecular mass (kDa) |
Oligomeric state | [Protein] @ refractometer μm | |
|---|---|---|---|---|
| Observed | Theoretical monomer | |||
| β1a | >1000 | Aggregate | ||
| 57.1 ± 1.1 | 57 | 1.00 | 0.27 | |
| β1a-core | >1000 | Aggregate | ||
| 104 ± 1 | 2.42 | 0.35 | ||
| 67 ± 0.8 | 1.56 | 0.89 | ||
| 38 ± 0.1 | 43 | 0.88 | 0.86 | |
| 29 ± 0.1 | Contaminant | |||
| β1a-SH3/GK | 35.2 ± 0.2 | 37.2 | 0.95 | 9.7 |
| β1a-hook | 11.0 | 9.6 | 1.14 | |
| BSAa | 200 ± 1.6 | 2.99 | 0.38 | |
| 132.8 ± 0.5 | 1.98 | 1.2 | ||
| 67.1 ± 0.1 | 67 | 1.00 | 6.8 | |
a BSA was not monomeric.