EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
    1.5.3.1 | 6000 |
- |
1 * 100000 + 1 * 42000 + 1 * 20000 + 1 * 6000, SDS-PAGE |
392391 |
| 1.5.3.1 | 10000 |
- |
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE |
392382 |
| 1.5.3.1 | 14000 |
- |
1 * 96000 + 1 * 45000 + 1 * 23000 + 1 * 14000, SDS-PAGE |
392377 |
| 1.5.3.1 | 20000 |
- |
1 * 100000 + 1 * 42000 + 1 * 20000 + 1 * 6000, SDS-PAGE |
392391 |
| 1.5.3.1 | 21000 |
- |
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE |
392382 |
| 1.5.3.1 | 23000 |
- |
1 * 96000 + 1 * 45000 + 1 * 23000 + 1 * 14000, SDS-PAGE |
392377 |
| 1.5.3.1 | 42000 |
- |
1 * 100000 + 1 * 42000 + 1 * 20000 + 1 * 6000, SDS-PAGE |
392391 |
| 1.5.3.1 | 42000 |
- |
gel filtration, SDS-PAGE |
392378 |
| 1.5.3.1 | 43000 |
- |
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration |
724937 |
| 1.5.3.1 | 43000 |
- |
x * 43000, calculated, x * 51000, SDS-PAGE |
671547 |
