[Detection of nonspecific proteolytic activity in a destabilase--endo-epsilon-(gamma-glutamyl)-lysyl-isopeptidase in the presence of SDS].
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.
Zavalova
L L
LL
Kuzina
E V
EV
Baskova
I P
IP
D000577:Amides / Q000378:metabolism; D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013379:Substrate Specificity
D000577:Amides; D005343:Fibrinolytic Agents; D012967:Sodium Dodecyl Sulfate; D010450:Endopeptidases; C045348:fibrin destabilase
Poiavlenie nespetsificheskoĭ proteoliticheskoĭ aktivnosti u destabilazy--éndo-epsilon-(gamma-glutamil)-lizil-izopeptidazy v prisutstvii Ds-Na.