EC Number   |
General Stability |
Reference |
|---|
    1.1.1.27 | addition of cofactor stabilizes all allozymes to urea inactivation |
286432 |
| 1.1.1.27 | fructose-1,6-diphosphate is necessary to stabilize the tetrameric enzyme form |
286452 |
| 1.1.1.27 | inactivation by pronase, trypsin and chymotrypsin |
286432 |
| 1.1.1.27 | irreversible loss of activity after several hours when the concentration is below 0.1 mg protein per ml |
286448 |
| 1.1.1.27 | Mn2+ and fructose 1,6-diphosphate are required during dialysis at pH 5.5, very unstable during dialysis at pH 7.5 although Mn2+ and fructose 1,6-diphosphate are added |
286448 |
| 1.1.1.27 | modification by o-phthalaldehyde not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding |
655742 |
| 1.1.1.27 | N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH |
654791 |
| 1.1.1.27 | NADH and fructose 1,6-diphosphate partially stabilize the 140000 Da molecular weight form against dissociation in triethanolamine-hydrochloride buffer at pH 8.0 |
286433 |
| 1.1.1.27 | PEG and trehalose stabilize the enzyme |
741355 |
| 1.1.1.27 | stable to dilution in the range 0.2-0.01 mg protein per ml |
286448 |
