EC Number   |
General Stability |
Reference |
|---|
    4.1.1.39 | at low H2O2 concentrations (0.2-10 mM), the properties of the enzyme (e.g., structure and susceptibility to heat denaturation) change slightly. At higher H2O2 concentrations (10-200 mM), rubisco undergoes an unfolding process, including the loss of secondary and tertiary structure, forming extended hydrophobic interface, and leading to cross links between large subunits. High concentrations of H2O2 can also result in an increase in susceptibility of rubisco to heat denaturation. Further pretreatments with or without reductive reagents to rubisco show that the disulfide bonds in rubisco help to protect the enzyme from damage by H2O2 as well as other reactive oxygen species |
661222 |
| 4.1.1.39 | bovine serum albumin stabilizes |
4452 |
| 4.1.1.39 | casein and leupeptin protect against proteolysis |
4466 |
| 4.1.1.39 | crude extracts instable, stabilization by MgSO4 or K2SO4 |
4473 |
| 4.1.1.39 | detergent, e.g. Triton X-100, Tween stabilizes |
4452 |
| 4.1.1.39 | monitoring the stability of Rubisco in micropropagated Vitis vinifera by two-dimensional electrophoresis |
662717 |
| 4.1.1.39 | when assayed in vitro, the enzyme itself exhibits a slow loss of activity even with saturating levels of all reaction components. This slow inactivation is facilitated by high temperature, low concentration of CO2 or Mg2+ and high O2 |
663032 |
