SummaryIn 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 α2-macroglobulin and α2-plasmin inhibitor which are antiactivators or fast reacting antiplasmins, and consequently, induced the activation of the fibrinolytic enzyme system in plasma.

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In the present study, an elastase-like enzyme which possessed elastolytic, proteolytic and N^α-Acetyl-L-tyrosine ethyl ester hydrolytic activities was extracted from skin lesions with Sweet’s syndrome.

It was comfirmed that elastase was liberated from pancreas into blood during acute pancreatitis and became combined with a2-macroglobulin. In the present study, elastase was purified from a 2-macroglobulin fractions of patient's plasma with acute pancreatitis and the activation mechanism of fibrinolytic enzyme