Increased stability of PEG-PPG conjugated human urokinase against autolysis.
Human urokinase (UK) was easily degraded during the incubation at 37 degrees C in a time-dependent manner. The degradation was also observed in the presence of trypsin inhibitors, suggesting that UK was not degraded by exogeneous trypsin-like serine protease but by autolysis. In this cases, the A-chain of UK was selectively degraded. Polyethylene glycol-polypropylene glycol conjugated urokinase (PEG-PPG-UK) was not degraded after prolonged incubation at 37 degrees C. These results demonstrated that PEG-PPG modification completely blocked the degradation of UK by autolysis.
Kajihara
J
J
Development Laboratory, JCR Pharmaceuticals Co., Ltd., Kobe, Japan.
Shibata
K
K
Kato
K
K
D001329:Autolysis / Q000378:metabolism*; D001665:Binding Sites; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011092:Polyethylene Glycols / Q000737:chemistry* / Q000378:metabolism; D011108:Polymers / Q000737:chemistry* / Q000378:metabolism; D011409:Propylene Glycols / Q000737:chemistry* / Q000378:metabolism; D014568:Urokinase-Type Plasminogen Activator / Q000737:chemistry* / Q000378:metabolism*
D003432:Cross-Linking Reagents; D011108:Polymers; D011409:Propylene Glycols; C012504:polypropylene glycol; D011092:Polyethylene Glycols; D014568:Urokinase-Type Plasminogen Activator