Abstract
Plasmin enzymatic activity in the presence of actin.
Highlights
Plasminogen/plasmin system takes part in a wide spectrum of physiological and pathophysiological processes in human organism, such as reproduction, embryogenesis, tissue remodeling, allergic and inflammatory reactions, carcinogenesis and metastasis formation
A key reaction of the fibrinolytic process is the conversion of plasminogen to the active serine protease plasmin (E.C.3.21.7)
The conversion of plasminogen in plasmin is the key process of fibrinolysis
Summary
Aim. To study the changes in the plasmin activity towards substrates with high and low molecular mass in the presence of actin. We have studied an interaction of biotinylated Glu-plasminogen and its fragments (kringle 1-3, kringle 4 and mini-plasminogen) with immobilized G-actin. Glu-plasminogen and kringle 4 had a high affinity towards actin (C50 is 113 and 117 nM correspondingly). A similar affinity of Glu-plasminogen and kringle 1-3 towards actin proves the involvement of the kringle 1-3 lysine-binding sites of the native plasminogen form in the actin interaction. Actin can modulate plasmin specificity towards high molecular mass substrates through its interaction with lysine-binding sites of the enzyme kringle domains. Actin inhibition of the fibrinolytic activity of plasmin is due to its competition with fibrin for thelysine binding sites of plasminogen/plasmin
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
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.
