EC Number   |
General Stability |
Reference |
|---|
   3.4.21.66 | Anionic protease, a component which frequently contaminates preparations of routinely isolated cationic protease, stabilizes thermitase |
29545 |
| 3.4.21.66 | Autolysis and thereby inactivation at elevated temperature, at alkaline pH-values and in the absence of added substrate |
29549 |
| 3.4.21.66 | Ca2+ stabilizes against both autolysis and thermal denaturation |
29549 |
| 3.4.21.66 | Irreversible inhibition by chloromethyl ketones causes marked stabilization against thermal denaturation, reversible inhibitors have no influence on stability |
29561 |
| 3.4.21.66 | The stability is significantly improved by 1 M acetate and chloride |
29563 |
| 3.4.21.66 | Unusually tight binding of Ca by thermitase emerges as the most likely single influence responsible for its increased thermostability |
29553 |
