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• W66677475 abstract "Physiological fibrinolysis is a proteolytic degradation of polymerized fibrin. A particular fibrinolytic enzyme system is present in blood. The central reaction in this system is the activation of a proenzyme, plasminogen, to the proteolytic enzyme plasmin. The activation is triggered by highly specialized proteases, plasminogen activators. One of these, the tissue plasminogen activator (tPA), is synthesized by endothelial cells and excreted to the blood on certain stimuli. Properties, which distinguish tPA from other types of plasminogen activators are a high affinity to fibrin and the very strong stimulation exerted by fibrin on tPA induced activation (2–3 orders of magnitude). These properties have evoked the idea of an efficient ternary activation complex between tPA, plasminogen and fibrin. The work on the isolation of tPA, the determination of its primary structure and gene structure as well as elucidation of its physicochemical properties has been performed by a large number of scientists. Several reviews have been published (e.g. Collen 1980; Ranby and Wallen 1985; Dano et al. 1985; Erickson et al. 1985; Wallen 1987). Fig. 1 shows the now well established primary structure* of wild tPA." @default.
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• W66677475 date "1990-01-01" @default.
• W66677475 modified "2023-09-27" @default.
• W66677475 title "Effects of Structural Modifications on the Properties of Tissue Plasminogen Activator (tPA)" @default.
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• W66677475 doi "https://doi.org/10.1007/978-1-4615-3806-6_18" @default.
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