EC Number   |
General Stability |
Reference |
|---|
    6.3.4.16 | acetylglutamate ATP accelerates the oxidative inactivation by mixtures of Fe3+, ascorbate, and O2 |
1472 |
| 6.3.4.16 | elastase inactivates. Addition of ATP, Mg2+, K+ and N-acetyl-L-glutamate protects entirely |
1451 |
| 6.3.4.16 | elastase inactivates. Addition of ATP, Mg2+, K+ and N-acetyl-L-glutamate protects entirely. Acetylglutamate alone speeds inactivation |
1451 |
| 6.3.4.16 | glycerol and DTT stabilize during purification |
1456 |
| 6.3.4.16 | inactivated by the Fe3+-oxygen-ascorbate model system for mixed-function oxidation. The susceptibility is markedly increased by acetylglutamate, when ATP is absent. ATP, and even more a mixture of ATP and bicarbonate protect from inactivation |
1458 |
| 6.3.4.16 | no inactivation by elastase |
1451 |
| 6.3.4.16 | stabilty under pressure, progressive inactivation down to 50% of initial activity at 200 MPa, this residual activity is constant at 200 MPa for at least 50 min |
722163 |
| 6.3.4.16 | trypsin, chymotrypsin, and papain also hydrolyze the oxidized enzyme considerybly faster than the native enzyme |
1458 |
