EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
    4.1.1.11 | 11000 |
- |
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine |
3950 |
| 4.1.1.11 | 13800 |
- |
x * 13800, SDS-PAGE |
682386 |
| 4.1.1.11 | 13800 |
- |
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine |
3950 |
| 4.1.1.11 | 14000 |
- |
4 * 14000 |
650836 |
| 4.1.1.11 | 14000 |
- |
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE |
650998 |
| 4.1.1.11 | 14100 |
- |
x * 14100, pi-protein, calculated from the amino acid sequence |
649350 |
| 4.1.1.11 | 16000 |
- |
4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE |
653749 |
| 4.1.1.11 | 40000 |
- |
gel filtration |
744560 |
| 4.1.1.11 | 41000 |
- |
SDS-PAGE |
744560 |
| 4.1.1.11 | 55600 |
- |
- |
728327 |
