| Abstrakt: |
The highly specific enzyme--destabilase [endo-epsilon-(gamma-glutamyl)- lysyl-isopeptidase]--similar to the true protease, acquires after incubation with sodium dodecyl sulfate a pronounced proteolytic activity towards certain proteins. At the same time, the amidolytic activity of the enzyme (substrate of p-nitroanilide gamma-glutamic acid) disappears, while its ability to catalyse the monomerization of the D-D dimer, a fragment of stabilized fibrin, is preserved. After SDS removal by gel filtration, the enzyme loses its nonspecific proteolytic activity, while its specific activity is fully reconstituted. Other detergents produce a more weak influence upon the enzyme. The putative mechanism providing the increase in the enzyme specificity in the presence of sodium dodecyl sulfate is discussed. |
