[Kinetic characteristics of the activation of various structural forms of plasminogen by tissue activator in the presence of fibrin].
It was shown that activation of two native plasminogen and miniplasminogen forms by the tissue activator in the presence of fibrin obeys the Michaelis-Menten kinetics. The kinetic parameters of activation of both plasminogen native forms differ insignificantly. For miniplasminogen whose molecule contains no lysine-binding sites, a marked decrease of activation power was observed. The Km value of activator for miniplasminogen is 10 times that of plasminogen form I and 20 times that of plasminogen form II. The kcat/Km value of activator for miniplasminogen is 7 times less than that of plasminogen form I and by one order of magnitude more than that of plasminogen form II. These results testify to the importance of lysine-binding sites in the native plasminogen molecule during the activation of fibrinolysis by the major physiological activator.
D005337:Fibrin / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010958:Plasminogen / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000502:physiology*
D005337:Fibrin; D010958:Plasminogen; D010959:Tissue Plasminogen Activator
Kineticheskaia kharakteristika aktivatsii razlichnykh strukturnykh form plazminogena tkanevym aktivatorom v prisutstvii fibrina.