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 con...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 51; no. 8; p. 1256
Main Authors Taran, L D, Makagonenko, E M, Nazarenko, N A, Kudinov, S A
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.08.1986
Subjects
Fibrin - metabolism
Glycosylation
Humans
In Vitro Techniques
Kinetics
Plasminogen - metabolism
Tissue Plasminogen Activator - physiology
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Summary: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.
ISSN:0320-9725