title: Studies on the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase.
abstract: 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.
mesh_terms: 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
chemical_list: D000979:alpha-2-Antiplasmin; D000511:alpha-Macroglobulins; D010958:Plasminogen; D014106:Tosylarginine Methyl Ester; D010960:Plasminogen Activators; D010196:Pancreatic Elastase; D014568:Urokinase-Type Plasminogen Activator