EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
   3.2.1.209 | 23000 |
- |
1 * 44000 + 1 * 23000, reducing SDS-PAGE |
135972 |
| 3.2.1.209 | 23000 |
- |
analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis |
677614 |
| 3.2.1.209 | 27000 |
- |
analytical electrophoresis of the purified preparation reveals two polypeptides |
679890 |
| 3.2.1.209 | 42000 |
- |
1 * 42000, SDS-PAGE |
646606 |
| 3.2.1.209 | 43000 |
- |
Candida albicans CAI-4 mutant generating an active 43 kDa polypeptide. Zymogram analysis shows that the single proteolytic product of 43 kDa is able to hydrolyze the fluorogenic substrate and, this is not observed when proteolysis is blocked by pepstatin |
677614 |
| 3.2.1.209 | 43000 |
- |
converting the 52 kDa alpha-mannosidase into a polypeptide of 43 kDa retaining full enzyme activity demonstrated in membranes of ATCC 26555, support a precursor-product relationship between soluble alpha1,2-mannosidase E-I (52 kDa) and alpha1,2-mannosidase E-II (43 kDa) |
679890 |
| 3.2.1.209 | 43000 |
- |
purified alpha-mannosidase E-II remains unaltered after treatment with aspartyl protease and retains full activity on artificial substrate 4-methylumbelliferyl-alpha-D-mannopyranoside |
677614 |
| 3.2.1.209 | 44000 |
- |
1 * 44000 + 1 * 23000, reducing SDS-PAGE |
135972 |
| 3.2.1.209 | 50000 |
- |
gel filtration |
646606 |
| 3.2.1.209 | 52000 |
- |
alpha1,2-mannosidase E-I. Analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis |
677614 |
