Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
