EC Number   |
General Stability |
Reference |
|---|
    1.4.1.4 | 1 mg/ml bovine serum albumin stabilizes |
391642 |
| 1.4.1.4 | 10 mM MOPS-NaOH pH 7.1 and 0.3-0.4 M NaCl is the best buffer |
391661 |
| 1.4.1.4 | 2-mercaptoethanol and dithiothreitol stabilizes |
391678 |
| 1.4.1.4 | 50% v/v glycerol and or bovine serum albumin in buffer enhances the stability, inactivated by freezing/thawing |
391677 |
| 1.4.1.4 | after incubation with chymotrypsin enzyme loses 50% activity within 30 min and a combination of 2-oxoglutarate and NADP+ affords near complete protection against chymotrypsin |
700335 |
| 1.4.1.4 | Aspergillus terreus NADP-GDH remains fully active even after 2 h of incubation with chymotrypsin |
700335 |
| 1.4.1.4 | elevated pressures up to 750 atm have a strong stabilizing effect on two extremely thermophilic glutamate dehydrogenases: the native enzyme from the hyperthermophile Pyrococcus furiosus, and a recombinant mutant enzyme containing an extra tetrapeptide at the C-terminus. The presence of the tetrapeptide greatly destabilizes the recombinant mutant at ambient pressure; however, the destabilizing effect is largely reversed by the application of pressure. Destabilization is due to weakened intersubunit ion-pair interactions induced by thermal fluctuations of the tetrapeptide. For both enzymes, the stabilizing effect of pressure increases with temperature as well as pressure, reaching 36fold for recombinant enzyme at 105°C and 750 atm |
723731 |
| 1.4.1.4 | Gdh3-encoded enzyme undergoes in vitro deamination at a particular asparaginyl residue which is absent in homologous isoenzyme, Gdh1p. Deamination of Asn54 is observed in vitro when Gdh3p is incubated at alkaline pH. The specific deamination of Asn54, could account, in part, for the relative lower stability of the GDH3-encoded protein |
654465 |
| 1.4.1.4 | in absence of salt it is irreversibly inactivated, optimal NaCl concentration is 1.1 M |
391682 |
| 1.4.1.4 | in presence of polyethyleneimine , the enzyme almost maintains the full initial activity after 2 h under conditions where the untreated enzyme retains only 20% of the initial activity, and the effect of the enzyme concentration on enzyme stability almost disappears. This stabilization is maintained in the pH range 59, but it is lost at high ionic strength. |
742408 |
