EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
   6.1.1.14 | -999 |
- |
primary structure of both subunits |
154 |
| 6.1.1.14 | 27000 |
- |
2-3 * 27000, about, partially processed isozyme GlyRS1, SDS-PAGE |
652111 |
| 6.1.1.14 | 30000 |
- |
2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE |
147 |
| 6.1.1.14 | 30000 |
- |
4 * 30000, about, partially processed isozyme GlyRS2, SDS-PAGE |
652111 |
| 6.1.1.14 | 33000 |
- |
2 * 33000 (alpha) + 2 * 80000 (beta), SDS-PAGE |
146 |
| 6.1.1.14 | 40000 |
- |
x * 40000 + x * 78000, alpha-alpha interactions contibute to the stability of the native enzyme while beta-beta interactions do not, SDS-PAGE |
149 |
| 6.1.1.14 | 51000 |
- |
x * 51000, SDS-PAGE |
651043 |
| 6.1.1.14 | 57500 |
- |
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE |
150 |
| 6.1.1.14 | 66000 |
- |
gel filtration, enzyme form E2 |
147 |
| 6.1.1.14 | 67600 |
- |
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE |
150 |
