EC Number   |
General Stability |
Reference |
|---|
   3.4.21.64 | Depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability and enhances the deactivation by 8 M urea |
29510 |
| 3.4.21.64 | interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation |
753872 |
| 3.4.21.64 | proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation |
707588 |
| 3.4.21.64 | Relatively resistant to SDS, 0.2% in 50 mM Tris/HCl, pH 7.4 |
29508 |
| 3.4.21.64 | Relatively stable towards heat and denaturing agents |
29501 |
| 3.4.21.64 | Urea, 4 M, stable |
29508 |
