EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
   1.10.3.3 | 62000 |
- |
1 * 74000 + 1 * 62000, SDS-PAGE |
439930 |
| 1.10.3.3 | 62258 |
- |
x * 62258, deduced from amino acid sequence |
439903 |
| 1.10.3.3 | 64000 |
- |
x * 64000, SDS-PAGE |
439903 |
| 1.10.3.3 | 65000 |
- |
2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE |
439925 |
| 1.10.3.3 | 70000 |
- |
2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively |
439890 |
| 1.10.3.3 | 70000 |
- |
4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview |
717986 |
| 1.10.3.3 | 72000 |
- |
2 * 72000, basic enzyme, SDS-PAGE |
439938 |
| 1.10.3.3 | 74000 |
- |
1 * 74000 + 1 * 62000, SDS-PAGE |
439930 |
| 1.10.3.3 | 80000 |
- |
- |
439929, 439932 |
| 1.10.3.3 | 132000 |
- |
gel filtration |
439925 |
