[Physico-chemical and enzymatic properties of polymeric trypsin derivatives based on dextran].
The molecular weight distribution, thermal stability during autolysis, resistance to human serum inhibitors as well as temperature optimum of native and dextran-modified trypsin were investigated. The seeming constants of autolytic inactivation and inhibition of native and modified trypsin were calculated. Trypsin polymer derivatives had higher molecular weight than the native enzyme. They also showed higher resistance to autolysis and serum inhibitors. Possible causes of the above effects are discussed.
D001329:Autolysis; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography; D002850:Chromatography, Gel; D003911:Dextrans; D013696:Temperature; D014357:Trypsin; D014361:Trypsin Inhibitors
D003911:Dextrans; D014361:Trypsin Inhibitors; D014357:Trypsin
Izuchenie nekotorykh fiziko-kimicheskik i énzimaticheskikh svoĭstv polimernykh proizvodnykh tripina na osnove dekstrana.