Studies on the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase.
In the present study, the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase was investigated. It was confirmed that human pancreatic elastase not only converted the co-existing plasminogen to low molecular weight-plasminogen which could be easily activated by the activator, but also inhibited alpha 2-macroglobulin and alpha 2-plasmin inhibitor which are antiactivators or fast reacting antiplasmins, and consequently, induced the activation of the fibrinolytic enzyme system in plasma.
D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005342:Fibrinolysis; D006801:Humans; D007185:Incubators; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000097:blood* / Q000494:pharmacology; D010958:Plasminogen / Q000378:metabolism; D010960:Plasminogen Activators / Q000378:metabolism; D013997:Time Factors; D014106:Tosylarginine Methyl Ester / Q000378:metabolism; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism; D000979:alpha-2-Antiplasmin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000302:isolation & purification
D000979:alpha-2-Antiplasmin; D000511:alpha-Macroglobulins; D010958:Plasminogen; D014106:Tosylarginine Methyl Ester; D010960:Plasminogen Activators; D010196:Pancreatic Elastase; D014568:Urokinase-Type Plasminogen Activator