EC Number   |
General Stability |
Reference |
|---|
    3.6.1.1 | 5 mM Mg2+ stabilizes, the midpoint of thermal denaturation is increased to 98°C |
678510 |
| 3.6.1.1 | decreasing activity at 4°C in reaction mixture lacking diphosphate , KCl prevents from inactivation, Mg-diphosphate, does not protect from inactivation |
209825 |
| 3.6.1.1 | extremely stable. No dissociation into subunit or unfolding of polypeptide chain occurrs in the presence of 8 M |
209827 |
| 3.6.1.1 | stability enhanced by bovine serum albumin or calmodulin |
209775 |
| 3.6.1.1 | unstable, but protected by cysteine, dithiothreitol, glutathione at pH 7.4 |
209779 |
| 3.6.1.1 | urea. Unfolding using guanidine-HC1 suggests that the transition between a native tetrameric state and an unfolded state is completely reversible, and essentially independent of any additional factors such as divalent metal cation or dithiothreitol |
209827 |
