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After human plasminogen activated by SK was partially reduced by dithioerythritol in the presence of plasmin-inhibitor leupeptin, a functionally active light (B)·SK complex was isolated by affinity chromatography with Lysine-Sepharose.This LB·SK complex shows a molecular weight of 60, 000 composed of LB 22, 000 and modified SK: 37, 000 by SDS-polyacrylamide gel electrophoresis.Results were as follows.1) Binding site to SK was located in the part of LB chain of human plasmin.2) Making complex with SK, amidolytic activity of LB·SK was increased twice to three times than that of LB itself.3) LB·SK complex showed both fibrinolytic and plasminogen activator activities and activated human, bovine and rabbit plasminogen to plasmin in spite of race difference.4) Thrombolytic activity of LB·SK complex had the most powerfull effect compared with SK, UK and human plasmin.

Preparation of light chain (plasmin)SK complex and its enzymatic properties.