[Purification and properties of plasminogen activator from human blood plasma after sudden death].

Plasminogen activator from human blood plasma after sudden death was isolated and purified 60-90-fold by precipitation with ammonium sulfate, ZnSO4 and ethanol as well as by chromatography on DEAE-Sephadex A-50 and gel--filtration through Sephadex G-200. The resulting enzyme had specific activity of 110-210 units per mg of protein. The enzyme prepartion possessed no plasmin activity; total content of carbohydrates was 2.4-2.5%; that of syalic acids--1.2-1.3%. The enzyme was found heterogeneous during disc electrophoresis in 7.0% polyacrylamide gel and corresponded in its mobility to beta-globulins of blood plasma. Molecular weight of enzyme as determined by gel-filtration through Sephadex G-200 is 70000. The isoelectric point lies at pH 6.2.