EC Number   |
Reference |
|---|
   2.7.3.2 | dose- and time-dependent inhibition by cystine, cysteamine prevents and reverses this inhibition |
671632 |
| 2.7.3.2 | enzyme, inactivated due to unfolding after treatment with lactic acid, refolds in presence of NaCl |
660930 |
| 2.7.3.2 | freeze drying leads to rearrangement of isozyme CK-MB after dissociation of the subunits |
660931 |
| 2.7.3.2 | inhibition of enzyme by sodium barbital may be reveresed by dilution |
671814 |
| 2.7.3.2 | insoluble recombinant enzyme from Escherichia coli by 6 M urea, unfolding shows biphasic kinetic courses, aggregation during refolding follows first-order kinetics, refolding intermediates are stabilized by NaCl, refolded enzyme shows high specific activity |
662723 |
| 2.7.3.2 | reactivation of 5,5'-dithiobis-(2-nitrobenzoic acid)-modified enzyme by excess of dithiothreitol, kinetics |
642428 |
| 2.7.3.2 | reactivators are thiols, like N-acetylcysteine, beta-mercaptoethanol, dithiothreitol, monothioglycerol, glutathione |
642388 |
| 2.7.3.2 | refolded in 50 mM Tris-HCl at pH 8.3 containing 500 mM NaCl and 5 mM dithiothreitol |
761710 |
| 2.7.3.2 | study on enzyme aggregation and reassociation in presence of sodium dodecyl sulfate-cyclodextrin. Aggregation does not occur at concentrations below 0.002 mM or temperature below 17°C. Trapping of monomeric creatine kinase variants such as thiol residue modified enzyme, sodium dodecyl sulfate binding enzyme, cyclodextrin treated enzyme, or dithiothreitol treated enzyme. Reassociation in presence of sodium dodecly sulfate-cyclodextrin follows first-order kinetics |
674947 |
| 2.7.3.2 | study on refolding of creatine kinase after denaturation with guanidine hydrochloride. Mixed macromolecular crowding agents, e.g. CT DNA and Ficoll 70, are more favorable and can reflect the physiological environment more accurately than single crowding agents |
675415 |
